Skip to main content
Microbiological Reviews logoLink to Microbiological Reviews
. 1983 Sep;47(3):313–344. doi: 10.1128/mr.47.3.313-344.1983

Mechanisms of protein localization.

T J Silhavy, S A Benson, S D Emr
PMCID: PMC281579  PMID: 6355805

Full text

PDF
343

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Achtman M., Manning P. A., Edelbluth C., Herrlich P. Export without proteolytic processing of inner and outer membrane proteins encoded by F sex factor tra cistrons in Escherichia coli minicells. Proc Natl Acad Sci U S A. 1979 Oct;76(10):4837–4841. doi: 10.1073/pnas.76.10.4837. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Ades I. Z., Butow R. A. The products of mitochondria-bound cytoplasmic polysomes in yeast. J Biol Chem. 1980 Oct 25;255(20):9918–9924. [PubMed] [Google Scholar]
  3. Alt F. W., Bothwell A. L., Knapp M., Siden E., Mather E., Koshland M., Baltimore D. Synthesis of secreted and membrane-bound immunoglobulin mu heavy chains is directed by mRNAs that differ at their 3' ends. Cell. 1980 Jun;20(2):293–301. doi: 10.1016/0092-8674(80)90615-7. [DOI] [PubMed] [Google Scholar]
  4. Bassford P. J., Jr, Silhavy T. J., Beckwith J. R. Use of gene fusion to study secretion of maltose-binding protein into Escherichia coli periplasm. J Bacteriol. 1979 Jul;139(1):19–31. doi: 10.1128/jb.139.1.19-31.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Bassford P., Beckwith J. Escherichia coli mutants accumulating the precursor of a secreted protein in the cytoplasm. Nature. 1979 Feb 15;277(5697):538–541. doi: 10.1038/277538a0. [DOI] [PubMed] [Google Scholar]
  6. Bedouelle H., Bassford P. J., Jr, Fowler A. V., Zabin I., Beckwith J., Hofnung M. Mutations which alter the function of the signal sequence of the maltose binding protein of Escherichia coli. Nature. 1980 May 8;285(5760):78–81. doi: 10.1038/285078a0. [DOI] [PubMed] [Google Scholar]
  7. Benson S. A., Silhavy T. J. Information within the mature LamB protein necessary for localization to the outer membrane of E coli K12. Cell. 1983 Apr;32(4):1325–1335. doi: 10.1016/0092-8674(83)90313-6. [DOI] [PubMed] [Google Scholar]
  8. Berg N. O., Eriksson S. Liver disease in adults with alpha-1 -antitrypsin deficiency. N Engl J Med. 1972 Dec 21;287(25):1264–1267. doi: 10.1056/NEJM197212212872502. [DOI] [PubMed] [Google Scholar]
  9. Blobel G., Dobberstein B. Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma. J Cell Biol. 1975 Dec;67(3):835–851. doi: 10.1083/jcb.67.3.835. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Blobel G., Dobberstein B. Transfer of proteins across membranes. II. Reconstitution of functional rough microsomes from heterologous components. J Cell Biol. 1975 Dec;67(3):852–862. doi: 10.1083/jcb.67.3.852. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Blobel G. Intracellular protein topogenesis. Proc Natl Acad Sci U S A. 1980 Mar;77(3):1496–1500. doi: 10.1073/pnas.77.3.1496. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Boeke J. D., Model P. A prokaryotic membrane anchor sequence: carboxyl terminus of bacteriophage f1 gene III protein retains it in the membrane. Proc Natl Acad Sci U S A. 1982 Sep;79(17):5200–5204. doi: 10.1073/pnas.79.17.5200. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Boeke J. D., Russel M., Model P. Processing of filamentous phage pre-coat protein. Effect of sequence variations near the signal peptidase cleavage site. J Mol Biol. 1980 Dec 5;144(2):103–116. doi: 10.1016/0022-2836(80)90027-3. [DOI] [PubMed] [Google Scholar]
  14. Bonatti S., Blobel G. Absence of a cleavable signal sequence in Sindbis virus glycoprotein PE2. J Biol Chem. 1979 Dec 25;254(24):12261–12264. [PubMed] [Google Scholar]
  15. Boyd A., Kendall K., Simon M. I. Structure of the serine chemoreceptor in Escherichia coli. Nature. 1983 Feb 17;301(5901):623–626. doi: 10.1038/301623a0. [DOI] [PubMed] [Google Scholar]
  16. Braell W. A., Lodish H. F. Biosynthesis of the erythrocyte anion transport protein. J Biol Chem. 1981 Nov 10;256(21):11337–11344. [PubMed] [Google Scholar]
  17. Braell W. A., Lodish H. F. Ovalbumin utilizes an NH2-terminal signal sequence. J Biol Chem. 1982 Apr 25;257(8):4578–4582. [PubMed] [Google Scholar]
  18. Braell W. A., Lodish H. F. The erythrocyte anion transport protein is contranslationally inserted into microsomes. Cell. 1982 Jan;28(1):23–31. doi: 10.1016/0092-8674(82)90371-3. [DOI] [PubMed] [Google Scholar]
  19. Braun V. Covalent lipoprotein from the outer membrane of Escherichia coli. Biochim Biophys Acta. 1975 Oct 31;415(3):335–377. doi: 10.1016/0304-4157(75)90013-1. [DOI] [PubMed] [Google Scholar]
  20. Bremer E., Beck E., Hindennach I., Sonntag I., Henning U. Cloned structural gene (ompA) for an integral outer membrane protein of Escherichia coli K-12: localization on hybrid plasmid pTU100 and expression of a fragment of the gene. Mol Gen Genet. 1980;179(1):13–20. doi: 10.1007/BF00268440. [DOI] [PubMed] [Google Scholar]
  21. Bremer E., Cole S. T., Hindennach I., Henning U., Beck E., Kurz C., Schaller H. Export of a protein into the outer membrane of Escherichia coli K12. Stable incorporation of the OmpA protein requires less than 193 amino-terminal amino-acid residues. Eur J Biochem. 1982 Feb;122(1):223–231. doi: 10.1111/j.1432-1033.1982.tb05870.x. [DOI] [PubMed] [Google Scholar]
  22. Cancedda R., Schlesinger M. J. Localization of polyribosomes containing alkaline phosphatase nascent polypeptides on membranes of Escherichia coli. J Bacteriol. 1974 Jan;117(1):290–301. doi: 10.1128/jb.117.1.290-301.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Casadaban M. J. Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu. J Mol Biol. 1976 Jul 5;104(3):541–555. doi: 10.1016/0022-2836(76)90119-4. [DOI] [PubMed] [Google Scholar]
  24. Chang C. N., Blobel G., Model P. Detection of prokaryotic signal peptidase in an Escherichia coli membrane fraction: endoproteolytic cleavage of nascent f1 pre-coat protein. Proc Natl Acad Sci U S A. 1978 Jan;75(1):361–365. doi: 10.1073/pnas.75.1.361. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Chang C. N., Model P., Blobel G. Membrane biogenesis: cotranslational integration of the bacteriophage f1 coat protein into an Escherichia coli membrane fraction. Proc Natl Acad Sci U S A. 1979 Mar;76(3):1251–1255. doi: 10.1073/pnas.76.3.1251. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Chou P. Y., Fasman G. D. Empirical predictions of protein conformation. Annu Rev Biochem. 1978;47:251–276. doi: 10.1146/annurev.bi.47.070178.001343. [DOI] [PubMed] [Google Scholar]
  27. Chua N. H., Schmidt G. W. Post-translational transport into intact chloroplasts of a precursor to the small subunit of ribulose-1,5-bisphosphate carboxylase. Proc Natl Acad Sci U S A. 1978 Dec;75(12):6110–6114. doi: 10.1073/pnas.75.12.6110. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Clément J. M., Hofnung M. Gene sequence of the lambda receptor, an outer membrane protein of E. coli K12. Cell. 1981 Dec;27(3 Pt 2):507–514. doi: 10.1016/0092-8674(81)90392-5. [DOI] [PubMed] [Google Scholar]
  29. Collins M. L., Niederman R. A. Membranes of Rhodospirillum rubrum: isolation and physicochemical properties of membranes from aerobically grown cells. J Bacteriol. 1976 Jun;126(3):1316–1325. doi: 10.1128/jb.126.3.1316-1325.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Crowlesmith I., Gamon K., Henning U. Precursor proteins are intermediates in vivo in the synthesis of two major outer membrane proteins, the OmpA and OmpF proteins, of Escherichia coli K12. Eur J Biochem. 1981 Jan;113(2):375–380. doi: 10.1111/j.1432-1033.1981.tb05076.x. [DOI] [PubMed] [Google Scholar]
  31. Daniels C. J., Bole D. G., Quay S. C., Oxender D. L. Role for membrane potential in the secretion of protein into the periplasm of Escherichia coli. Proc Natl Acad Sci U S A. 1981 Sep;78(9):5396–5400. doi: 10.1073/pnas.78.9.5396. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Dassa E., Boquet P. L. ExpA: a conditional mutation affecting the expression of a group of exported proteins in Escherichia coli K-12. Mol Gen Genet. 1981;181(2):192–200. doi: 10.1007/BF00268426. [DOI] [PubMed] [Google Scholar]
  33. Date T. Demonstration by a novel genetic technique that leader peptidase is an essential enzyme of Escherichia coli. J Bacteriol. 1983 Apr;154(1):76–83. doi: 10.1128/jb.154.1.76-83.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Date T., Goodman J. M., Wickner W. T. Procoat, the precursor of M13 coat protein, requires an electrochemical potential for membrane insertion. Proc Natl Acad Sci U S A. 1980 Aug;77(8):4669–4673. doi: 10.1073/pnas.77.8.4669. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Date T., Wickner W. Isolation of the Escherichia coli leader peptidase gene and effects of leader peptidase overproduction in vivo. Proc Natl Acad Sci U S A. 1981 Oct;78(10):6106–6110. doi: 10.1073/pnas.78.10.6106. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Date T., Zwizinski C., Ludmerer S., Wickner W. Mechanisms of membrane assembly: effects of energy poisons on the conversion of soluble M13 coliphage procoat to membrane-bound coat protein. Proc Natl Acad Sci U S A. 1980 Feb;77(2):827–831. doi: 10.1073/pnas.77.2.827. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Daum G., Gasser S. M., Schatz G. Import of proteins into mitochondria. Energy-dependent, two-step processing of the intermembrane space enzyme cytochrome b2 by isolated yeast mitochondria. J Biol Chem. 1982 Nov 10;257(21):13075–13080. [PubMed] [Google Scholar]
  38. Davis B. D., Tai P. C. The mechanism of protein secretion across membranes. Nature. 1980 Jan 31;283(5746):433–438. doi: 10.1038/283433a0. [DOI] [PubMed] [Google Scholar]
  39. DiRienzo J. M., Inouye M. Lipid fluidity-dependent biosynthesis and assembly of the outer membrane proteins of E. coli. Cell. 1979 May;17(1):155–161. doi: 10.1016/0092-8674(79)90303-9. [DOI] [PubMed] [Google Scholar]
  40. DiRienzo J. M., Nakamura K., Inouye M. The outer membrane proteins of Gram-negative bacteria: biosynthesis, assembly, and functions. Annu Rev Biochem. 1978;47:481–532. doi: 10.1146/annurev.bi.47.070178.002405. [DOI] [PubMed] [Google Scholar]
  41. Dobberstein B., Blobel G., Chua N. H. In vitro synthesis and processing of a putative precursor for the small subunit of ribulose-1,5-bisphosphate carboxylase of Chlamydomonas reinhardtii. Proc Natl Acad Sci U S A. 1977 Mar;74(3):1082–1085. doi: 10.1073/pnas.74.3.1082. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. Drickamer L. K. Fragmentation of the 95,000-dalton transmembrane polypeptide in human erythrocyte membranes. J Biol Chem. 1976 Sep 10;251(17):5115–5123. [PubMed] [Google Scholar]
  43. Drickamer L. K. Fragmentation of the band 3 polypeptide from human erythrocyte membranes. Identification of regions likely to interact with the lipid bilayer. J Biol Chem. 1977 Oct 10;252(19):6909–6917. [PubMed] [Google Scholar]
  44. Drickamer L. K. Orientation of the band 3 polypeptide from human erythrocyte membranes. Identification of NH2-terminal sequence and site of carbohydrate attachment. J Biol Chem. 1978 Oct 25;253(20):7242–7248. [PubMed] [Google Scholar]
  45. Early P., Rogers J., Davis M., Calame K., Bond M., Wall R., Hood L. Two mRNAs can be produced from a single immunoglobulin mu gene by alternative RNA processing pathways. Cell. 1980 Jun;20(2):313–319. doi: 10.1016/0092-8674(80)90617-0. [DOI] [PubMed] [Google Scholar]
  46. Ehring R., Beyreuther K., Wright J. K., Overath P. In vitro and in vivo products of E. coli lactose permease gene are identical. Nature. 1980 Feb 7;283(5747):537–540. doi: 10.1038/283537a0. [DOI] [PubMed] [Google Scholar]
  47. Emr S. D., Bassford P. J., Jr Localization and processing of outer membrane and periplasmic proteins in Escherichia coli strains harboring export-specific suppressor mutations. J Biol Chem. 1982 May 25;257(10):5852–5860. [PubMed] [Google Scholar]
  48. Emr S. D., Hall M. N., Silhavy T. J. A mechanism of protein localization: the signal hypothesis and bacteria. J Cell Biol. 1980 Sep;86(3):701–711. doi: 10.1083/jcb.86.3.701. [DOI] [PMC free article] [PubMed] [Google Scholar]
  49. Emr S. D., Hanley-Way S., Silhavy T. J. Suppressor mutations that restore export of a protein with a defective signal sequence. Cell. 1981 Jan;23(1):79–88. doi: 10.1016/0092-8674(81)90272-5. [DOI] [PubMed] [Google Scholar]
  50. Emr S. D., Hedgpeth J., Clément J. M., Silhavy T. J., Hofnung M. Sequence analysis of mutations that prevent export of lambda receptor, an Escherichia coli outer membrane protein. Nature. 1980 May 8;285(5760):82–85. doi: 10.1038/285082a0. [DOI] [PubMed] [Google Scholar]
  51. Emr S. D., Schwartz M., Silhavy T. J. Mutations altering the cellular localization of the phage lambda receptor, an Escherichia coli outer membrane protein. Proc Natl Acad Sci U S A. 1978 Dec;75(12):5802–5806. doi: 10.1073/pnas.75.12.5802. [DOI] [PMC free article] [PubMed] [Google Scholar]
  52. Emr S. D., Silhavy T. J. Importance of secondary structure in the signal sequence for protein secretion. Proc Natl Acad Sci U S A. 1983 Aug;80(15):4599–4603. doi: 10.1073/pnas.80.15.4599. [DOI] [PMC free article] [PubMed] [Google Scholar]
  53. Emr S. D., Silhavy T. J. Molecular components of the signal sequence that function in the initiation of protein export. J Cell Biol. 1982 Dec;95(3):689–696. doi: 10.1083/jcb.95.3.689. [DOI] [PMC free article] [PubMed] [Google Scholar]
  54. Emr S. D., Silhavy T. J. Mutations affecting localization of an Escherichia coli outer membrane protein, the bacteriophage lambda receptor. J Mol Biol. 1980 Jul 25;141(1):63–90. doi: 10.1016/s0022-2836(80)80029-5. [DOI] [PubMed] [Google Scholar]
  55. Filip C., Fletcher G., Wulff J. L., Earhart C. F. Solubilization of the cytoplasmic membrane of Escherichia coli by the ionic detergent sodium-lauryl sarcosinate. J Bacteriol. 1973 Sep;115(3):717–722. doi: 10.1128/jb.115.3.717-722.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  56. Fischer H. D., Gonzalez-Noriega A., Sly W. S. Beta-glucuronidase binding to human fibroblast membrane receptors. J Biol Chem. 1980 Jun 10;255(11):5069–5074. [PubMed] [Google Scholar]
  57. Fox C. F., Law J. H., Tsukagoshi N., Wilson G. A density label for membranes. Proc Natl Acad Sci U S A. 1970 Oct;67(2):598–605. doi: 10.1073/pnas.67.2.598. [DOI] [PMC free article] [PubMed] [Google Scholar]
  58. Fraser T. H., Bruce B. J. Chicken ovalbumin is synthesized and secreted by Escherichia coli. Proc Natl Acad Sci U S A. 1978 Dec;75(12):5936–5940. doi: 10.1073/pnas.75.12.5936. [DOI] [PMC free article] [PubMed] [Google Scholar]
  59. Frazer A. C., Curtiss R., 3rd Production, properties and utility of bacterial minicells. Curr Top Microbiol Immunol. 1975;69:1–84. doi: 10.1007/978-3-642-50112-8_1. [DOI] [PubMed] [Google Scholar]
  60. Freitag H., Janes M., Neupert W. Biosynthesis of mitochondrial porin and insertion into the outer mitochondrial membrane of Neurospora crassa. Eur J Biochem. 1982 Aug;126(1):197–202. doi: 10.1111/j.1432-1033.1982.tb06766.x. [DOI] [PubMed] [Google Scholar]
  61. Fukuda M., Eshdat Y., Tarone G., Marchesi V. T. Isolation and characterization of peptides derived from the cytoplasmic segment of band 3, the predominant intrinsic membrane protein of the human erythrocyte. J Biol Chem. 1978 Apr 10;253(7):2419–2428. [PubMed] [Google Scholar]
  62. Gasser S. M., Ohashi A., Daum G., Böhni P. C., Gibson J., Reid G. A., Yonetani T., Schatz G. Imported mitochondrial proteins cytochrome b2 and cytochrome c1 are processed in two steps. Proc Natl Acad Sci U S A. 1982 Jan;79(2):267–271. doi: 10.1073/pnas.79.2.267. [DOI] [PMC free article] [PubMed] [Google Scholar]
  63. Gething M. J., Sambrook J. Construction of influenza haemagglutinin genes that code for intracellular and secreted forms of the protein. Nature. 1982 Dec 16;300(5893):598–603. doi: 10.1038/300598a0. [DOI] [PubMed] [Google Scholar]
  64. Gibson R., Schlesinger S., Kornfeld S. The nonglycosylated glycoprotein of vesicular stomatitis virus is temperature-sensitive and undergoes intracellular aggregation at elevated temperatures. J Biol Chem. 1979 May 10;254(9):3600–3607. [PubMed] [Google Scholar]
  65. Gilmore R., Walter P., Blobel G. Protein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptor. J Cell Biol. 1982 Nov;95(2 Pt 1):470–477. doi: 10.1083/jcb.95.2.470. [DOI] [PMC free article] [PubMed] [Google Scholar]
  66. Goodman J. M., Watts C., Wickner W. Membrane assembly: posttranslational insertion of M13 procoat protein into E. coli membranes and its proteolytic conversion to coat protein in vitro. Cell. 1981 May;24(2):437–441. doi: 10.1016/0092-8674(81)90334-2. [DOI] [PubMed] [Google Scholar]
  67. Halegoua S., Inouye M. Translocation and assembly of outer membrance proteins of Escherichia coli. Selective accumulation of precursors and novel assembly intermediates caused by phenethyl alcohol. J Mol Biol. 1979 May 5;130(1):39–61. doi: 10.1016/0022-2836(79)90551-5. [DOI] [PubMed] [Google Scholar]
  68. Hall M. N., Gabay J., Débarbouillé M., Schwartz M. A role for mRNA secondary structure in the control of translation initiation. Nature. 1982 Feb 18;295(5850):616–618. doi: 10.1038/295616a0. [DOI] [PubMed] [Google Scholar]
  69. Hall M. N., Gabay J., Schwartz M. Evidence for a coupling of synthesis and export of an outer membrane protein in Escherichia coli. EMBO J. 1983;2(1):15–19. doi: 10.1002/j.1460-2075.1983.tb01373.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  70. Hall M. N., Schwartz M., Silhavy T. J. Sequence information within the lamB genes in required for proper routing of the bacteriophage lambda receptor protein to the outer membrane of Escherichia coli K-12. J Mol Biol. 1982 Mar 25;156(1):93–112. doi: 10.1016/0022-2836(82)90461-2. [DOI] [PubMed] [Google Scholar]
  71. Hall M. N., Silhavy T. J. Genetic analysis of the major outer membrane proteins of Escherichia coli. Annu Rev Genet. 1981;15:91–142. doi: 10.1146/annurev.ge.15.120181.000515. [DOI] [PubMed] [Google Scholar]
  72. Hall M. N., Silhavy T. J. The ompB locus and the regulation of the major outer membrane porin proteins of Escherichia coli K12. J Mol Biol. 1981 Feb 15;146(1):23–43. doi: 10.1016/0022-2836(81)90364-8. [DOI] [PubMed] [Google Scholar]
  73. Hallermayer G., Zimmermann R., Neupert W. Kinetic studies on the transport of cytoplasmically synthesized proteins into the mitochondria in intact cells of Neurospora crassa. Eur J Biochem. 1977 Dec;81(3):523–532. doi: 10.1111/j.1432-1033.1977.tb11978.x. [DOI] [PubMed] [Google Scholar]
  74. Hasilik A., Neufeld E. F. Biosynthesis of lysosomal enzymes in fibroblasts. Phosphorylation of mannose residues. J Biol Chem. 1980 May 25;255(10):4946–4950. [PubMed] [Google Scholar]
  75. Hasilik A., Neufeld E. F. Biosynthesis of lysosomal enzymes in fibroblasts. Synthesis as precursors of higher molecular weight. J Biol Chem. 1980 May 25;255(10):4937–4945. [PubMed] [Google Scholar]
  76. Hedgpeth J., Clement J. M., Marchal C., Perrin D., Hofnung M. DNA sequence encoding the NH2-terminal peptide involved in transport of lambda receptor, an Escherichia coli secretory protein. Proc Natl Acad Sci U S A. 1980 May;77(5):2621–2625. doi: 10.1073/pnas.77.5.2621. [DOI] [PMC free article] [PubMed] [Google Scholar]
  77. Hennig B., Neupert W. Assembly of cytochrome c. Apocytochrome c is bound to specific sites on mitochondria before its conversion to holocytochrome c. Eur J Biochem. 1981 Dec;121(1):203–212. doi: 10.1111/j.1432-1033.1981.tb06450.x. [DOI] [PubMed] [Google Scholar]
  78. Hickman S., Shapiro L. J., Neufeld E. F. A recognition marker required for uptake of a lysosomal enzyme by cultured fibroblasts. Biochem Biophys Res Commun. 1974 Mar 15;57(1):55–61. doi: 10.1016/s0006-291x(74)80356-6. [DOI] [PubMed] [Google Scholar]
  79. Higgins C. F., Haag P. D., Nikaido K., Ardeshir F., Garcia G., Ames G. F. Complete nucleotide sequence and identification of membrane components of the histidine transport operon of S. typhimurium. Nature. 1982 Aug 19;298(5876):723–727. doi: 10.1038/298723a0. [DOI] [PubMed] [Google Scholar]
  80. Hussain M., Ichihara S., Mizushima S. Accumulation of glyceride-containing precursor of the outer membrane lipoprotein in the cytoplasmic membrane of Escherichia coli treated with globomycin. J Biol Chem. 1980 Apr 25;255(8):3707–3712. [PubMed] [Google Scholar]
  81. Hussain M., Ichihara S., Mizushima S. Mechanism of signal peptide cleavage in the biosynthesis of the major lipoprotein of the Escherichia coli outer membrane. J Biol Chem. 1982 May 10;257(9):5177–5182. [PubMed] [Google Scholar]
  82. Ichihara S., Hussain M., Mizushima S. Characterization of new membrane lipoproteins and their precursors of Escherichia coli. J Biol Chem. 1981 Mar 25;256(6):3125–3129. [PubMed] [Google Scholar]
  83. Inouye H., Barnes W., Beckwith J. Signal sequence of alkaline phosphatase of Escherichia coli. J Bacteriol. 1982 Feb;149(2):434–439. doi: 10.1128/jb.149.2.434-439.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  84. Inouye H., Beckwith J. Synthesis and processing of an Escherichia coli alkaline phosphatase precursor in vitro. Proc Natl Acad Sci U S A. 1977 Apr;74(4):1440–1444. doi: 10.1073/pnas.74.4.1440. [DOI] [PMC free article] [PubMed] [Google Scholar]
  85. Inouye M., Halegoua S. Secretion and membrane localization of proteins in Escherichia coli. CRC Crit Rev Biochem. 1980;7(4):339–371. doi: 10.3109/10409238009105465. [DOI] [PubMed] [Google Scholar]
  86. Inouye S., Soberon X., Franceschini T., Nakamura K., Itakura K., Inouye M. Role of positive charge on the amino-terminal region of the signal peptide in protein secretion across the membrane. Proc Natl Acad Sci U S A. 1982 Jun;79(11):3438–3441. doi: 10.1073/pnas.79.11.3438. [DOI] [PMC free article] [PubMed] [Google Scholar]
  87. Inouye S., Wang S., Sekizawa J., Halegoua S., Inouye M. Amino acid sequence for the peptide extension on the prolipoprotein of the Escherichia coli outer membrane. Proc Natl Acad Sci U S A. 1977 Mar;74(3):1004–1008. doi: 10.1073/pnas.74.3.1004. [DOI] [PMC free article] [PubMed] [Google Scholar]
  88. Ito K., Beckwith J. R. Role of the mature protein sequence of maltose-binding protein in its secretion across the E. coli cytoplasmic membrane. Cell. 1981 Jul;25(1):143–150. doi: 10.1016/0092-8674(81)90238-5. [DOI] [PubMed] [Google Scholar]
  89. Ito K. Purification of the precursor form of maltose-binding protein, a periplasmic protein of Escherichia coli. J Biol Chem. 1982 Sep 10;257(17):9895–9897. [PubMed] [Google Scholar]
  90. Ito K., Sato T., Yura T. Synthesis and assembly of the membrane proteins in E. coli. Cell. 1977 Jul;11(3):551–559. doi: 10.1016/0092-8674(77)90073-3. [DOI] [PubMed] [Google Scholar]
  91. Ito K., Wittekind M., Nomura M., Shiba K., Yura T., Miura A., Nashimoto H. A temperature-sensitive mutant of E. coli exhibiting slow processing of exported proteins. Cell. 1983 Mar;32(3):789–797. doi: 10.1016/0092-8674(83)90065-x. [DOI] [PubMed] [Google Scholar]
  92. Jamieson J. D., Palade G. E. Intracellular transport of secretory proteins in the pancreatic exocrine cell. I. Role of the peripheral elements of the Golgi complex. J Cell Biol. 1967 Aug;34(2):577–596. doi: 10.1083/jcb.34.2.577. [DOI] [PMC free article] [PubMed] [Google Scholar]
  93. Jamieson J. D., Palade G. E. Intracellular transport of secretory proteins in the pancreatic exocrine cell. II. Transport to condensing vacuoles and zymogen granules. J Cell Biol. 1967 Aug;34(2):597–615. doi: 10.1083/jcb.34.2.597. [DOI] [PMC free article] [PubMed] [Google Scholar]
  94. Jaskunas S. R., Fallon A. M., Nomura M. Identification and organization of ribosomal protein genes of Escherichia coli carried by lambdafus2 transducing phage. J Biol Chem. 1977 Oct 25;252(20):7323–7336. [PubMed] [Google Scholar]
  95. Jaskunas S. R., Fallon A. M., Nomura M., Williams B. G., Blattner F. R. Expression of ribosomal protein genes cloned in Charon vector phages and identification of their promoters. J Biol Chem. 1977 Oct 25;252(20):7355–7364. [PubMed] [Google Scholar]
  96. Josefsson L. G., Randall L. L. Different exported proteins in E. coli show differences in the temporal mode of processing in vivo. Cell. 1981 Jul;25(1):151–157. doi: 10.1016/0092-8674(81)90239-7. [DOI] [PubMed] [Google Scholar]
  97. Josefsson L. G., Randall L. L. Processing in vivo of precursor maltose-binding protein in Escherichia coli occurs post-translationally as well as co-translationally. J Biol Chem. 1981 Mar 10;256(5):2504–2507. [PubMed] [Google Scholar]
  98. Kaplan A., Achord D. T., Sly W. S. Phosphohexosyl components of a lysosomal enzyme are recognized by pinocytosis receptors on human fibroblasts. Proc Natl Acad Sci U S A. 1977 May;74(5):2026–2030. doi: 10.1073/pnas.74.5.2026. [DOI] [PMC free article] [PubMed] [Google Scholar]
  99. Katz F. N., Rothman J. E., Knipe D. M., Lodish H. F. Membrane assembly: synthesis and intracellular processing of the vesicular stomatitis viral glycoprotein. J Supramol Struct. 1977;7(3-4):353–370. doi: 10.1002/jss.400070308. [DOI] [PubMed] [Google Scholar]
  100. Katz F. N., Rothman J. E., Lingappa V. R., Blobel G., Lodish H. F. Membrane assembly in vitro: synthesis, glycosylation, and asymmetric insertion of a transmembrane protein. Proc Natl Acad Sci U S A. 1977 Aug;74(8):3278–3282. doi: 10.1073/pnas.74.8.3278. [DOI] [PMC free article] [PubMed] [Google Scholar]
  101. Kehry M., Ewald S., Douglas R., Sibley C., Raschke W., Fambrough D., Hood L. The immunoglobulin mu chains of membrane-bound and secreted IgM molecules differ in their C-terminal segments. Cell. 1980 Sep;21(2):393–406. doi: 10.1016/0092-8674(80)90476-6. [DOI] [PubMed] [Google Scholar]
  102. Koshland D., Botstein D. Evidence for posttranslational translocation of beta-lactamase across the bacterial inner membrane. Cell. 1982 Oct;30(3):893–902. doi: 10.1016/0092-8674(82)90294-x. [DOI] [PubMed] [Google Scholar]
  103. Koshland D., Botstein D. Secretion of beta-lactamase requires the carboxy end of the protein. Cell. 1980 Jul;20(3):749–760. doi: 10.1016/0092-8674(80)90321-9. [DOI] [PubMed] [Google Scholar]
  104. Koshland D., Sauer R. T., Botstein D. Diverse effects of mutations in the signal sequence on the secretion of beta-lactamase in Salmonella typhimurium. Cell. 1982 Oct;30(3):903–914. doi: 10.1016/0092-8674(82)90295-1. [DOI] [PubMed] [Google Scholar]
  105. Kreibich G., Czakó-Graham M., Grebenau R., Mok W., Rodriguez-Boulan E., Sabatini D. D. Characterization of the ribosomal binding site in rat liver rough microsomes: ribophorins I and II, two integral membrane proteins related to ribosome binding. J Supramol Struct. 1978;8(3):279–302. doi: 10.1002/jss.400080307. [DOI] [PubMed] [Google Scholar]
  106. Kreil G. Transfer of proteins across membranes. Annu Rev Biochem. 1981;50:317–348. doi: 10.1146/annurev.bi.50.070181.001533. [DOI] [PubMed] [Google Scholar]
  107. Kumamoto C. A., Beckwith J. Mutations in a new gene, secB, cause defective protein localization in Escherichia coli. J Bacteriol. 1983 Apr;154(1):253–260. doi: 10.1128/jb.154.1.253-260.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  108. Lai J. S., Sarvas M., Brammar W. J., Neugebauer K., Wu H. C. Bacillus licheniformis penicillinase synthesized in Escherichia coli contains covalently linked fatty acid and glyceride. Proc Natl Acad Sci U S A. 1981 Jun;78(6):3506–3510. doi: 10.1073/pnas.78.6.3506. [DOI] [PMC free article] [PubMed] [Google Scholar]
  109. Lazdunski C., Baty D., Pagès J. M. Procaine, a local anesthetic interacting with the cell membrane, inhibits the processing of precursor forms of periplasmic proteins in Escherichia coli. Eur J Biochem. 1979 May 2;96(1):49–57. doi: 10.1111/j.1432-1033.1979.tb13012.x. [DOI] [PubMed] [Google Scholar]
  110. Lin J. J., Kanazawa H., Ozols J., Wu H. C. An Escherichia coli mutant with an amino acid alteration within the signal sequence of outer membrane prolipoprotein. Proc Natl Acad Sci U S A. 1978 Oct;75(10):4891–4895. doi: 10.1073/pnas.75.10.4891. [DOI] [PMC free article] [PubMed] [Google Scholar]
  111. Lindahl L., Post L., Zengel J., Gilbert S. F., Strycharz W. A., Nomura M. Mapping of ribosomal protein genes by in vitro protein synthesis using DNA fragments of lambdafus3 transducing phage DNA as templates. J Biol Chem. 1977 Oct 25;252(20):7365–7383. [PubMed] [Google Scholar]
  112. Lingappa V. R., Katz F. N., Lodish H. F., Blobel G. A signal sequence for the insertion of a transmembrane glycoprotein. Similarities to the signals of secretory proteins in primary structure and function. J Biol Chem. 1978 Dec 25;253(24):8667–8670. [PubMed] [Google Scholar]
  113. Lingappa V. R., Lingappa J. R., Blobel G. Chicken ovalbumin contains an internal signal sequence. Nature. 1979 Sep 13;281(5727):117–121. doi: 10.1038/281117a0. [DOI] [PubMed] [Google Scholar]
  114. Lingappa V. R., Shields D., Woo S. L., Blobel G. Nascent chicken ovalbumin contains the functional equivalent of a signal sequence. J Cell Biol. 1978 Nov;79(2 Pt 1):567–572. doi: 10.1083/jcb.79.2.567. [DOI] [PMC free article] [PubMed] [Google Scholar]
  115. Lodish H. F., Rothman J. E. The assembly of cell membranes. Sci Am. 1979 Jan;240(1):48–63. doi: 10.1038/scientificamerican0179-48. [DOI] [PubMed] [Google Scholar]
  116. Mandel G., Wickner W. Translational and post-translational cleavage of M13 procoat protein: extracts of both the cytoplasmic and outer membranes of Escherichia coli contain leader peptidase activity. Proc Natl Acad Sci U S A. 1979 Jan;76(1):236–240. doi: 10.1073/pnas.76.1.236. [DOI] [PMC free article] [PubMed] [Google Scholar]
  117. Matsuura S., Arpin M., Hannum C., Margoliash E., Sabatini D. D., Morimoto T. In vitro synthesis and posttranslational uptake of cytochrome c into isolated mitochondria: role of a specific addressing signal in the apocytochrome. Proc Natl Acad Sci U S A. 1981 Jul;78(7):4368–4372. doi: 10.1073/pnas.78.7.4368. [DOI] [PMC free article] [PubMed] [Google Scholar]
  118. McAda P. C., Douglas M. G. A neutral metallo endoprotease involved in the processing of an F1-ATPase subunit precursor in mitochondria. J Biol Chem. 1982 Mar 25;257(6):3177–3182. [PubMed] [Google Scholar]
  119. Meyer D. I., Dobberstein B. Identification and characterization of a membrane component essential for the translocation of nascent proteins across the membrane of the endoplasmic reticulum. J Cell Biol. 1980 Nov;87(2 Pt 1):503–508. doi: 10.1083/jcb.87.2.503. [DOI] [PMC free article] [PubMed] [Google Scholar]
  120. Meyer D. I., Krause E., Dobberstein B. Secretory protein translocation across membranes-the role of the "docking protein'. Nature. 1982 Jun 24;297(5868):647–650. doi: 10.1038/297647a0. [DOI] [PubMed] [Google Scholar]
  121. Michaelis S., Beckwith J. Mechanism of incorporation of cell envelope proteins in Escherichia coli. Annu Rev Microbiol. 1982;36:435–465. doi: 10.1146/annurev.mi.36.100182.002251. [DOI] [PubMed] [Google Scholar]
  122. Michaelis S., Guarente L., Beckwith J. In vitro construction and characterization of phoA-lacZ gene fusions in Escherichia coli. J Bacteriol. 1983 Apr;154(1):356–365. doi: 10.1128/jb.154.1.356-365.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  123. Michaelis S., Inouye H., Oliver D., Beckwith J. Mutations that alter the signal sequence of alkaline phosphatase in Escherichia coli. J Bacteriol. 1983 Apr;154(1):366–374. doi: 10.1128/jb.154.1.366-374.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  124. Milstein C., Brownlee G. G., Harrison T. M., Mathews M. B. A possible precursor of immunoglobulin light chains. Nat New Biol. 1972 Sep 27;239(91):117–120. doi: 10.1038/newbio239117a0. [DOI] [PubMed] [Google Scholar]
  125. Miura T., Mizushima S. Separation by density gradient centrifugation of two types of membranes from spheroplast membrane of Escherichia coli K12. Biochim Biophys Acta. 1968 Jan 3;150(1):159–161. doi: 10.1016/0005-2736(68)90020-5. [DOI] [PubMed] [Google Scholar]
  126. Moreno F., Fowler A. V., Hall M., Silhavy T. J., Zabin I., Schwartz M. A signal sequence is not sufficient to lead beta-galactosidase out of the cytoplasm. Nature. 1980 Jul 24;286(5771):356–359. doi: 10.1038/286356a0. [DOI] [PubMed] [Google Scholar]
  127. Mori M., Miura S., Tatibana M., Cohen P. P. Characterization of a protease apparently involved in processing of pre-ornithine transcarbamylase of rat liver. Proc Natl Acad Sci U S A. 1980 Dec;77(12):7044–7048. doi: 10.1073/pnas.77.12.7044. [DOI] [PMC free article] [PubMed] [Google Scholar]
  128. Mosmann T. R., Williamson A. R. Structural mutations in a mouse immunoglobulin light chain resulting in failure to be secreted. Cell. 1980 Jun;20(2):283–292. doi: 10.1016/0092-8674(80)90614-5. [DOI] [PubMed] [Google Scholar]
  129. Müller M., Ibrahimi I., Chang C. N., Walter P., Blobel G. A bacterial secretory protein requires signal recognition particle for translocation across mammalian endoplasmic reticulum. J Biol Chem. 1982 Oct 25;257(20):11860–11863. [PubMed] [Google Scholar]
  130. Neu H. C., Heppel L. A. The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts. J Biol Chem. 1965 Sep;240(9):3685–3692. [PubMed] [Google Scholar]
  131. Nielsen J., Hansen F. G., Hoppe J., Friedl P., von Meyenburg K. The nucleotide sequence of the atp genes coding for the F0 subunits a, b, c and the F1 subunit delta of the membrane bound ATP synthase of Escherichia coli. Mol Gen Genet. 1981;184(1):33–39. doi: 10.1007/BF00271191. [DOI] [PubMed] [Google Scholar]
  132. Novick P., Ferro S., Schekman R. Order of events in the yeast secretory pathway. Cell. 1981 Aug;25(2):461–469. doi: 10.1016/0092-8674(81)90064-7. [DOI] [PubMed] [Google Scholar]
  133. Novick P., Field C., Schekman R. Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell. 1980 Aug;21(1):205–215. doi: 10.1016/0092-8674(80)90128-2. [DOI] [PubMed] [Google Scholar]
  134. Novick P., Schekman R. Secretion and cell-surface growth are blocked in a temperature-sensitive mutant of Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1979 Apr;76(4):1858–1862. doi: 10.1073/pnas.76.4.1858. [DOI] [PMC free article] [PubMed] [Google Scholar]
  135. Oliver D. B., Beckwith J. E. coli mutant pleiotropically defective in the export of secreted proteins. Cell. 1981 Sep;25(3):765–772. doi: 10.1016/0092-8674(81)90184-7. [DOI] [PubMed] [Google Scholar]
  136. Oliver D. B., Beckwith J. Identification of a new gene (secA) and gene product involved in the secretion of envelope proteins in Escherichia coli. J Bacteriol. 1982 May;150(2):686–691. doi: 10.1128/jb.150.2.686-691.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  137. Oliver D. B., Beckwith J. Regulation of a membrane component required for protein secretion in Escherichia coli. Cell. 1982 Aug;30(1):311–319. doi: 10.1016/0092-8674(82)90037-x. [DOI] [PubMed] [Google Scholar]
  138. Oliver D., Kumamoto C., Quinlan M., Beckwith J. Pleiotropic mutants affecting the secretory apparatus of Escherichia coli. Ann Microbiol (Paris) 1982 Jan;133A(1):105–110. [PubMed] [Google Scholar]
  139. Osborn M. J., Gander J. E., Parisi E., Carson J. Mechanism of assembly of the outer membrane of Salmonella typhimurium. Isolation and characterization of cytoplasmic and outer membrane. J Biol Chem. 1972 Jun 25;247(12):3962–3972. [PubMed] [Google Scholar]
  140. Osborn M. J., Munson R. Separation of the inner (cytoplasmic) and outer membranes of Gram-negative bacteria. Methods Enzymol. 1974;31:642–653. doi: 10.1016/0076-6879(74)31070-1. [DOI] [PubMed] [Google Scholar]
  141. Osborn M. J., Wu H. C. Proteins of the outer membrane of gram-negative bacteria. Annu Rev Microbiol. 1980;34:369–422. doi: 10.1146/annurev.mi.34.100180.002101. [DOI] [PubMed] [Google Scholar]
  142. Ozols J., Gerard C. Primary structure of the membranous segment of cytochrome b5. Proc Natl Acad Sci U S A. 1977 Sep;74(9):3725–3729. doi: 10.1073/pnas.74.9.3725. [DOI] [PMC free article] [PubMed] [Google Scholar]
  143. Pagès J. M., Piovant M., Varenne S., Lazdunski C. Mechanistic aspects of the transfer of nascent periplasmic proteins across the cytoplasmic membrane in Escherichia coli. Eur J Biochem. 1978 May 16;86(2):589–602. doi: 10.1111/j.1432-1033.1978.tb12343.x. [DOI] [PubMed] [Google Scholar]
  144. Palade G. Intracellular aspects of the process of protein synthesis. Science. 1975 Aug 1;189(4200):347–358. doi: 10.1126/science.1096303. [DOI] [PubMed] [Google Scholar]
  145. Palmiter R. D., Gagnon J., Walsh K. A. Ovalbumin: a secreted protein without a transient hydrophobic leader sequence. Proc Natl Acad Sci U S A. 1978 Jan;75(1):94–98. doi: 10.1073/pnas.75.1.94. [DOI] [PMC free article] [PubMed] [Google Scholar]
  146. Palva E. T., Hirst T. R., Hardy S. J., Holmgren J., Randall L. Synthesis of a precursor to the B subunit of heat-labile enterotoxin in Escherichia coli. J Bacteriol. 1981 Apr;146(1):325–330. doi: 10.1128/jb.146.1.325-330.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  147. Pearse B. M. Clathrin: a unique protein associated with intracellular transfer of membrane by coated vesicles. Proc Natl Acad Sci U S A. 1976 Apr;73(4):1255–1259. doi: 10.1073/pnas.73.4.1255. [DOI] [PMC free article] [PubMed] [Google Scholar]
  148. Post L. E., Arfsten A. E., Davis G. R., Nomura M. DNA sequence of the promoter region for the alpha ribosomal protein operon in Escherichia coli. J Biol Chem. 1980 May 25;255(10):4653–4659. [PubMed] [Google Scholar]
  149. Pratt J. M., Holland I. B., Spratt B. G. Precursor forms of penicillin-binding proteins 5 and 6 of E. coli cytoplasmic membrane. Nature. 1981 Sep 24;293(5830):307–309. doi: 10.1038/293307a0. [DOI] [PubMed] [Google Scholar]
  150. Randall L. L., Hardy S. J. Synthesis of exported proteins by membrane-bound polysomes from Escherichia coli. Eur J Biochem. 1977 May 2;75(1):43–53. doi: 10.1111/j.1432-1033.1977.tb11502.x. [DOI] [PubMed] [Google Scholar]
  151. Rao A., Reithmeier R. A. Reactive sulfhydryl groups of the band 3 polypeptide from human erythroycte membranes. Location in the primary structure. J Biol Chem. 1979 Jul 10;254(13):6144–6150. [PubMed] [Google Scholar]
  152. Redman C. M., Sabatini D. D. Vectorial discharge of peptides released by puromycin from attached ribosomes. Proc Natl Acad Sci U S A. 1966 Aug;56(2):608–615. doi: 10.1073/pnas.56.2.608. [DOI] [PMC free article] [PubMed] [Google Scholar]
  153. Redman C. M., Siekevitz P., Palade G. E. Synthesis and transfer of amylase in pigeon pancreatic micromosomes. J Biol Chem. 1966 Mar 10;241(5):1150–1158. [PubMed] [Google Scholar]
  154. Reid G. A., Schatz G. Import of proteins into mitochondria. Extramitochondrial pools and post-translational import of mitochondrial protein precursors in vivo. J Biol Chem. 1982 Nov 10;257(21):13062–13067. [PubMed] [Google Scholar]
  155. Rogers J., Early P., Carter C., Calame K., Bond M., Hood L., Wall R. Two mRNAs with different 3' ends encode membrane-bound and secreted forms of immunoglobulin mu chain. Cell. 1980 Jun;20(2):303–312. doi: 10.1016/0092-8674(80)90616-9. [DOI] [PubMed] [Google Scholar]
  156. Roggenkamp R., Kustermann-Kuhn B., Hollenberg C. P. Expression and processing of bacterial beta-lactamase in the yeast Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1981 Jul;78(7):4466–4470. doi: 10.1073/pnas.78.7.4466. [DOI] [PMC free article] [PubMed] [Google Scholar]
  157. Rothman J. E., Fine R. E. Coated vesicles transport newly synthesized membrane glycoproteins from endoplasmic reticulum to plasma membrane in two successive stages. Proc Natl Acad Sci U S A. 1980 Feb;77(2):780–784. doi: 10.1073/pnas.77.2.780. [DOI] [PMC free article] [PubMed] [Google Scholar]
  158. Rothman J. E., Lodish H. F. Synchronised transmembrane insertion and glycosylation of a nascent membrane protein. Nature. 1977 Oct 27;269(5631):775–780. doi: 10.1038/269775a0. [DOI] [PubMed] [Google Scholar]
  159. Russel M., Model P. A mutation downstream from the signal peptidase cleavage site affects cleavage but not membrane insertion of phage coat protein. Proc Natl Acad Sci U S A. 1981 Mar;78(3):1717–1721. doi: 10.1073/pnas.78.3.1717. [DOI] [PMC free article] [PubMed] [Google Scholar]
  160. Ryter A., Shuman H., Schwartz M. Intergration of the receptor for bacteriophage lambda in the outer membrane of Escherichia coli: coupling with cell division. J Bacteriol. 1975 Apr;122(1):295–301. doi: 10.1128/jb.122.1.295-301.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  161. SIEKEVITZ P., PALADE G. E. A cytochemical study on the pancreas of the guinea pig. 5. In vivo incorporation of leucine-1-C14 into the chymotrypsinogen of various cell fractions. J Biophys Biochem Cytol. 1960 Jul;7:619–630. doi: 10.1083/jcb.7.4.619. [DOI] [PMC free article] [PubMed] [Google Scholar]
  162. Sabatini D. D., Blobel G. Controlled proteolysis of nascent polypeptides in rat liver cell fractions. II. Location of the polypeptides in rough microsomes. J Cell Biol. 1970 Apr;45(1):146–157. doi: 10.1083/jcb.45.1.146. [DOI] [PMC free article] [PubMed] [Google Scholar]
  163. Sabatini D. D., Kreibich G., Morimoto T., Adesnik M. Mechanisms for the incorporation of proteins in membranes and organelles. J Cell Biol. 1982 Jan;92(1):1–22. doi: 10.1083/jcb.92.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  164. Sancar A., Hack A. M., Rupp W. D. Simple method for identification of plasmid-coded proteins. J Bacteriol. 1979 Jan;137(1):692–693. doi: 10.1128/jb.137.1.692-693.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  165. Sando G. N., Neufeld E. F. Recognition and receptor-mediated uptake of a lysosomal enzyme, alpha-l-iduronidase, by cultured human fibroblasts. Cell. 1977 Nov;12(3):619–627. doi: 10.1016/0092-8674(77)90262-8. [DOI] [PubMed] [Google Scholar]
  166. Schatz G., Butow R. A. How are proteins imported into mitochondria? Cell. 1983 Feb;32(2):316–318. doi: 10.1016/0092-8674(83)90450-6. [DOI] [PubMed] [Google Scholar]
  167. Schechter I. Partial amino acid sequence of the precursor of immunoglobulin light chain programmed by messenger RNA in vitro. Science. 1975 Apr 11;188(4184):160–162. doi: 10.1126/science.803715. [DOI] [PubMed] [Google Scholar]
  168. Schedl P., Primakoff P. Mutants of Escherichia coli thermosensitive for the synthesis of transfer RNA. Proc Natl Acad Sci U S A. 1973 Jul;70(7):2091–2095. doi: 10.1073/pnas.70.7.2091. [DOI] [PMC free article] [PubMed] [Google Scholar]
  169. Schleyer M., Schmidt B., Neupert W. Requirement of a membrane potential for the posttranslational transfer of proteins into mitochondria. Eur J Biochem. 1982 Jun 15;125(1):109–116. doi: 10.1111/j.1432-1033.1982.tb06657.x. [DOI] [PubMed] [Google Scholar]
  170. Schmidt G. W., Devillers-Thiery A., Desruisseaux H., Blobel G., Chua N. H. NH2-terminal amino acid sequences of precursor and mature forms of the ribulose-1,5-bisphosphate carboxylase small subunit from Chlamydomonas reinhardtii. J Cell Biol. 1979 Dec;83(3):615–622. doi: 10.1083/jcb.83.3.615. [DOI] [PMC free article] [PubMed] [Google Scholar]
  171. Schnaitman C. A. Effect of ethylenediaminetetraacetic acid, Triton X-100, and lysozyme on the morphology and chemical composition of isolate cell walls of Escherichia coli. J Bacteriol. 1971 Oct;108(1):553–563. doi: 10.1128/jb.108.1.553-563.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  172. Schnaitman C. A. Protein composition of the cell wall and cytoplasmic membrane of Escherichia coli. J Bacteriol. 1970 Nov;104(2):890–901. doi: 10.1128/jb.104.2.890-901.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  173. Schwartz M., Roa M., Débarbouillé M. Mutations that affect lamB gene expression at a posttranscriptional level. Proc Natl Acad Sci U S A. 1981 May;78(5):2937–2941. doi: 10.1073/pnas.78.5.2937. [DOI] [PMC free article] [PubMed] [Google Scholar]
  174. Shultz J., Silhavy T. J., Berman M. L., Fiil N., Emr S. D. A previously unidentified gene in the spc operon of Escherichia coli K12 specifies a component of the protein export machinery. Cell. 1982 Nov;31(1):227–235. doi: 10.1016/0092-8674(82)90422-6. [DOI] [PubMed] [Google Scholar]
  175. Shuman H. A., Silhavy T. J., Beckwith J. R. Labeling of proteins with beta-galactosidase by gene fusion. Identification of a cytoplasmic membrane component of the Escherichia coli maltose transport system. J Biol Chem. 1980 Jan 10;255(1):168–174. [PubMed] [Google Scholar]
  176. Silhavy T. J., Casadaban M. J., Shuman H. A., Beckwith J. R. Conversion of beta-galactosidase to a membrane-bound state by gene fusion. Proc Natl Acad Sci U S A. 1976 Oct;73(10):3423–3427. doi: 10.1073/pnas.73.10.3423. [DOI] [PMC free article] [PubMed] [Google Scholar]
  177. Silhavy T. J., Shuman H. A., Beckwith J., Schwartz M. Use of gene fusions to study outer membrane protein localization in Escherichia coli. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5411–5415. doi: 10.1073/pnas.74.12.5411. [DOI] [PMC free article] [PubMed] [Google Scholar]
  178. Silver P., Watts C., Wickner W. Membrane assembly from purified components. I. Isolated M13 procoat does not require ribosomes or soluble proteins for processing by membranes. Cell. 1981 Aug;25(2):341–345. doi: 10.1016/0092-8674(81)90052-0. [DOI] [PubMed] [Google Scholar]
  179. Smith W. P. Cotranslational secretion of diphtheria toxin and alkaline phosphatase in vitro: involvement of membrane protein(s). J Bacteriol. 1980 Mar;141(3):1142–1147. doi: 10.1128/jb.141.3.1142-1147.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  180. Smith W. P., Tai P. C., Davis B. D. Bacillus licheniformis penicillinase: cleavages and attachment of lipid during cotranslational secretion. Proc Natl Acad Sci U S A. 1981 Jun;78(6):3501–3505. doi: 10.1073/pnas.78.6.3501. [DOI] [PMC free article] [PubMed] [Google Scholar]
  181. Smith W. P., Tai P. C., Thompson R. C., Davis B. D. Extracellular labeling of nascent polypeptides traversing the membrane of Escherichia coli. Proc Natl Acad Sci U S A. 1977 Jul;74(7):2830–2834. doi: 10.1073/pnas.74.7.2830. [DOI] [PMC free article] [PubMed] [Google Scholar]
  182. Steck T. L., Koziarz J. J., Singh M. K., Reddy G., Köhler H. Preparation and analysis of seven major, topographically defined fragments of band 3, the predominant transmembrane polypeptide of human erythrocyte membranes. Biochemistry. 1978 Apr 4;17(7):1216–1222. doi: 10.1021/bi00600a013. [DOI] [PubMed] [Google Scholar]
  183. Steck T. L., Ramos B., Strapazon E. Proteolytic dissection of band 3, the predominant transmembrane polypeptide of the human erythrocyte membrane. Biochemistry. 1976 Mar 9;15(5):1153–1161. doi: 10.1021/bi00650a030. [DOI] [PubMed] [Google Scholar]
  184. Steck T. L. The band 3 protein of the human red cell membrane: a review. J Supramol Struct. 1978;8(3):311–324. doi: 10.1002/jss.400080309. [DOI] [PubMed] [Google Scholar]
  185. Stevens T., Esmon B., Schekman R. Early stages in the yeast secretory pathway are required for transport of carboxypeptidase Y to the vacuole. Cell. 1982 Sep;30(2):439–448. doi: 10.1016/0092-8674(82)90241-0. [DOI] [PubMed] [Google Scholar]
  186. Struck D. K., Siuta P. B., Lane M. D., Lennarz W. J. Effect of tunicamycin on the secretion of serum proteins by primary cultures of rat and chick hepatocytes. Studies on transferrin, very low density lipoprotein, and serum albumin. J Biol Chem. 1978 Aug 10;253(15):5332–5337. [PubMed] [Google Scholar]
  187. Sugimoto K., Sugisaki H., Okamoto T., Takanami M. Studies on bacteriophage fd DNA. IV. The sequence of messenger RNA for the major coat protein gene. J Mol Biol. 1977 Apr 25;111(4):487–507. doi: 10.1016/s0022-2836(77)80065-x. [DOI] [PubMed] [Google Scholar]
  188. Suissa M., Schatz G. Import of proteins into mitochondria. Translatable mRNAs for imported mitochondrial proteins are present in free as well as mitochondria-bound cytoplasmic polysomes. J Biol Chem. 1982 Nov 10;257(21):13048–13055. [PubMed] [Google Scholar]
  189. Sutcliffe J. G. Nucleotide sequence of the ampicillin resistance gene of Escherichia coli plasmid pBR322. Proc Natl Acad Sci U S A. 1978 Aug;75(8):3737–3741. doi: 10.1073/pnas.75.8.3737. [DOI] [PMC free article] [PubMed] [Google Scholar]
  190. Sveda M. M., Markoff L. J., Lai C. J. Cell surface expression of the influenza virus hemagglutinin requires the hydrophobic carboxy-terminal sequences. Cell. 1982 Sep;30(2):649–656. doi: 10.1016/0092-8674(82)90261-6. [DOI] [PubMed] [Google Scholar]
  191. Talmadge K., Brosius J., Gilbert W. An 'internal' signal sequence directs secretion and processing or proinsulin in bacteria. Nature. 1981 Nov 12;294(5837):176–178. doi: 10.1038/294176a0. [DOI] [PubMed] [Google Scholar]
  192. Talmadge K., Stahl S., Gilbert W. Eukaryotic signal sequence transports insulin antigen in Escherichia coli. Proc Natl Acad Sci U S A. 1980 Jun;77(6):3369–3373. doi: 10.1073/pnas.77.6.3369. [DOI] [PMC free article] [PubMed] [Google Scholar]
  193. Tokunaga M., Loranger J. M., Wolfe P. B., Wu H. C. Prolipoprotein signal peptidase in Escherichia coli is distinct from the M13 procoat protein signal peptidase. J Biol Chem. 1982 Sep 10;257(17):9922–9925. [PubMed] [Google Scholar]
  194. Tokunaga M., Tokunaga H., Wu H. C. Post-translational modification and processing of Escherichia coli prolipoprotein in vitro. Proc Natl Acad Sci U S A. 1982 Apr;79(7):2255–2259. doi: 10.1073/pnas.79.7.2255. [DOI] [PMC free article] [PubMed] [Google Scholar]
  195. Tsuji T., Irimura T., Osawa T. The carbohydrate moiety of band-3 glycoprotein of human erythrocyte membranes. Biochem J. 1980 Jun 1;187(3):677–686. doi: 10.1042/bj1870677. [DOI] [PMC free article] [PubMed] [Google Scholar]
  196. Walter P., Blobel G. Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum. Proc Natl Acad Sci U S A. 1980 Dec;77(12):7112–7116. doi: 10.1073/pnas.77.12.7112. [DOI] [PMC free article] [PubMed] [Google Scholar]
  197. Walter P., Blobel G. Signal recognition particle contains a 7S RNA essential for protein translocation across the endoplasmic reticulum. Nature. 1982 Oct 21;299(5885):691–698. doi: 10.1038/299691a0. [DOI] [PubMed] [Google Scholar]
  198. Walter P., Blobel G. Translocation of proteins across the endoplasmic reticulum III. Signal recognition protein (SRP) causes signal sequence-dependent and site-specific arrest of chain elongation that is released by microsomal membranes. J Cell Biol. 1981 Nov;91(2 Pt 1):557–561. doi: 10.1083/jcb.91.2.557. [DOI] [PMC free article] [PubMed] [Google Scholar]
  199. Wandersman C., Moreno F., Schwartz M. Pleiotropic mutations rendering Escherichia coli K-12 resistant to bacteriophage TP1. J Bacteriol. 1980 Sep;143(3):1374–1383. doi: 10.1128/jb.143.3.1374-1383.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  200. Watts C., Silver P., Wickner W. Membrane assembly from purified components. II. Assembly of M13 procoat into liposomes reconstituted with purified leader peptidase. Cell. 1981 Aug;25(2):347–353. doi: 10.1016/0092-8674(81)90053-2. [DOI] [PubMed] [Google Scholar]
  201. White J., Helenius A. pH-dependent fusion between the Semliki Forest virus membrane and liposomes. Proc Natl Acad Sci U S A. 1980 Jun;77(6):3273–3277. doi: 10.1073/pnas.77.6.3273. [DOI] [PMC free article] [PubMed] [Google Scholar]
  202. Wickner W. Assembly of proteins into membranes. Science. 1980 Nov 21;210(4472):861–868. doi: 10.1126/science.7001628. [DOI] [PubMed] [Google Scholar]
  203. Wickner W. Asymmetric orientation of phage M13 coat protein in Escherichia coli cytoplasmic membranes and in synthetic lipid vesicles. Proc Natl Acad Sci U S A. 1976 Apr;73(4):1159–1163. doi: 10.1073/pnas.73.4.1159. [DOI] [PMC free article] [PubMed] [Google Scholar]
  204. Wickner W. The assembly of proteins into biological membranes: The membrane trigger hypothesis. Annu Rev Biochem. 1979;48:23–45. doi: 10.1146/annurev.bi.48.070179.000323. [DOI] [PubMed] [Google Scholar]
  205. Williams D. G., Jenkins R. E., Tanner M. J. Structure of the anion-transport protein of the human erythrocyte membrane. Further studies on the fragments produced by proteolytic digestion. Biochem J. 1979 Aug 1;181(2):477–493. doi: 10.1042/bj1810477. [DOI] [PMC free article] [PubMed] [Google Scholar]
  206. Wirth D. F., Lodish H. F., Robbins P. W. Requirements for the insertion of the Sindbis envelope glycoproteins into the endoplasmic reticulum membrane. J Cell Biol. 1979 Apr;81(1):154–162. doi: 10.1083/jcb.81.1.154. [DOI] [PMC free article] [PubMed] [Google Scholar]
  207. Wolfe P. B., Silver P., Wickner W. The isolation of homogeneous leader peptidase from a strain of Escherichia coli which overproduces the enzyme. J Biol Chem. 1982 Jul 10;257(13):7898–7902. [PubMed] [Google Scholar]
  208. Wu H. C., Lin J. J. Escherichia coli mutants altered in murein lipoprotein. J Bacteriol. 1976 Apr;126(1):147–156. doi: 10.1128/jb.126.1.147-156.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  209. Yamagata H., Ippolito C., Inukai M., Inouye M. Temperature-sensitive processing of outer membrane lipoprotein in an Escherichia coli mutant. J Bacteriol. 1982 Dec;152(3):1163–1168. doi: 10.1128/jb.152.3.1163-1168.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  210. Zilberstein A., Snider M. D., Porter M., Lodish H. F. Mutants of vesicular stomatitis virus blocked at different stages in maturation of the viral glycoprotein. Cell. 1980 Sep;21(2):417–427. doi: 10.1016/0092-8674(80)90478-x. [DOI] [PubMed] [Google Scholar]
  211. Zimmermann R., Neupert W. Transport of proteins into mitochondria. Posttranslational transfer of ADP/ATP carrier into mitochondria in vitro. Eur J Biochem. 1980 Aug;109(1):217–229. doi: 10.1111/j.1432-1033.1980.tb04787.x. [DOI] [PubMed] [Google Scholar]
  212. Zimmermann R., Paluch U., Neupert W. Cell-free synthesis of cytochrome c. FEBS Lett. 1979 Dec 1;108(1):141–146. doi: 10.1016/0014-5793(79)81196-5. [DOI] [PubMed] [Google Scholar]
  213. Zitomer R. S., Hall B. D. Yeast cytochrome c messenger RNA. In vitro translation and specific immunoprecipitation of the CYC1 gene product. J Biol Chem. 1976 Oct 25;251(20):6320–6326. [PubMed] [Google Scholar]
  214. Zwizinski C., Date T., Wickner W. Leader peptidase is found in both the inner and outer membranes of Escherichia coli. J Biol Chem. 1981 Apr 10;256(7):3593–3597. [PubMed] [Google Scholar]
  215. Zwizinski C., Wickner W. Purification and characterization of leader (signal) peptidase from Escherichia coli. J Biol Chem. 1980 Aug 25;255(16):7973–7977. [PubMed] [Google Scholar]

Articles from Microbiological Reviews are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES