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. 1993 Oct;175(19):6113–6117. doi: 10.1128/jb.175.19.6113-6117.1993

Processing of lipid-modified prolipoprotein requires energy and sec gene products in vivo.

N Kosic 1, M Sugai 1, C K Fan 1, H C Wu 1
PMCID: PMC206704  PMID: 8407783

Abstract

The kinetics of processing of glyceride-modified prolipoprotein that accumulated in globomycin-treated Escherichia coli has been found to be affected by sec mutations, i.e., secA, secE, secY, secD, and secF, and by metabolic poisons which affect proton motive force (PMF). The effect of sec mutations on processing of glyceride-modified prolipoprotein in vivo was not due to a secondary effect on PMF. Neither a secF mutation nor metabolic poisons affected the processing of previously accumulated proOmpA protein in vivo, suggesting that the requirements for functional sec gene products and PMF are specific to the processing of lipoprotein precursors by signal peptidase II.

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Selected References

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  1. Akiyama Y., Ito K. Export of Escherichia coli alkaline phosphatase attached to an integral membrane protein, SecY. J Biol Chem. 1989 Jan 5;264(1):437–442. [PubMed] [Google Scholar]
  2. Bieker K. L., Phillips G. J., Silhavy T. J. The sec and prl genes of Escherichia coli. J Bioenerg Biomembr. 1990 Jun;22(3):291–310. doi: 10.1007/BF00763169. [DOI] [PubMed] [Google Scholar]
  3. Braun V., Rehn K. Chemical characterization, spatial distribution and function of a lipoprotein (murein-lipoprotein) of the E. coli cell wall. The specific effect of trypsin on the membrane structure. Eur J Biochem. 1969 Oct;10(3):426–438. doi: 10.1111/j.1432-1033.1969.tb00707.x. [DOI] [PubMed] [Google Scholar]
  4. 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]
  5. Chen L., Tai P. C. Effects of antibiotics and other inhibitors on ATP-dependent protein translocation into membrane vesicles. J Bacteriol. 1987 Jun;169(6):2373–2379. doi: 10.1128/jb.169.6.2373-2379.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Dalbey R. E., Wickner W. Leader peptidase catalyzes the release of exported proteins from the outer surface of the Escherichia coli plasma membrane. J Biol Chem. 1985 Dec 15;260(29):15925–15931. [PubMed] [Google Scholar]
  7. Dev I. K., Ray P. H. Rapid assay and purification of a unique signal peptidase that processes the prolipoprotein from Escherichia coli B. J Biol Chem. 1984 Sep 10;259(17):11114–11120. [PubMed] [Google Scholar]
  8. Gardel C., Benson S., Hunt J., Michaelis S., Beckwith J. secD, a new gene involved in protein export in Escherichia coli. J Bacteriol. 1987 Mar;169(3):1286–1290. doi: 10.1128/jb.169.3.1286-1290.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Gardel C., Johnson K., Jacq A., Beckwith J. The secD locus of E.coli codes for two membrane proteins required for protein export. EMBO J. 1990 Oct;9(10):3209–3216. doi: 10.1002/j.1460-2075.1990.tb07519.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Hayashi S., Wu H. C. Lipoproteins in bacteria. J Bioenerg Biomembr. 1990 Jun;22(3):451–471. doi: 10.1007/BF00763177. [DOI] [PubMed] [Google Scholar]
  11. 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]
  12. Inada T., Court D. L., Ito K., Nakamura Y. Conditionally lethal amber mutations in the leader peptidase gene of Escherichia coli. J Bacteriol. 1989 Jan;171(1):585–587. doi: 10.1128/jb.171.1.585-587.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Inukai M., Takeuchi M., Shimizu K., Arai M. Mechanism of action of globomycin. J Antibiot (Tokyo) 1978 Nov;31(11):1203–1205. doi: 10.7164/antibiotics.31.1203. [DOI] [PubMed] [Google Scholar]
  14. Ito K., Date T., Wickner W. Synthesis, assembly into the cytoplasmic membrane, and proteolytic processing of the precursor of coliphage M13 coat protein. J Biol Chem. 1980 Mar 10;255(5):2123–2130. [PubMed] [Google Scholar]
  15. 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]
  16. Kobayashi H., Kin E., Anraku Y. Transport of sugars and amino acids in bacteria. X. Sources of energy and energy coupling reactions of the active transport systems for isoleucine and proline in E. coli. J Biochem. 1974 Aug;76(2):251–261. doi: 10.1093/oxfordjournals.jbchem.a130567. [DOI] [PubMed] [Google Scholar]
  17. 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]
  18. Kumamoto C. A. Molecular chaperones and protein translocation across the Escherichia coli inner membrane. Mol Microbiol. 1991 Jan;5(1):19–22. doi: 10.1111/j.1365-2958.1991.tb01821.x. [DOI] [PubMed] [Google Scholar]
  19. Muñoa F. J., Miller K. W., Beers R., Graham M., Wu H. C. Membrane topology of Escherichia coli prolipoprotein signal peptidase (signal peptidase II). J Biol Chem. 1991 Sep 15;266(26):17667–17672. [PubMed] [Google Scholar]
  20. 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]
  21. Oliver D. B., Cabelli R. J., Dolan K. M., Jarosik G. P. Azide-resistant mutants of Escherichia coli alter the SecA protein, an azide-sensitive component of the protein export machinery. Proc Natl Acad Sci U S A. 1990 Nov;87(21):8227–8231. doi: 10.1073/pnas.87.21.8227. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Riggs P. D., Derman A. I., Beckwith J. A mutation affecting the regulation of a secA-lacZ fusion defines a new sec gene. Genetics. 1988 Apr;118(4):571–579. doi: 10.1093/genetics/118.4.571. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. San Millan J. L., Boyd D., Dalbey R., Wickner W., Beckwith J. Use of phoA fusions to study the topology of the Escherichia coli inner membrane protein leader peptidase. J Bacteriol. 1989 Oct;171(10):5536–5541. doi: 10.1128/jb.171.10.5536-5541.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Schatz P. J., Riggs P. D., Jacq A., Fath M. J., Beckwith J. The secE gene encodes an integral membrane protein required for protein export in Escherichia coli. Genes Dev. 1989 Jul;3(7):1035–1044. doi: 10.1101/gad.3.7.1035. [DOI] [PubMed] [Google Scholar]
  25. Schägger H., von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem. 1987 Nov 1;166(2):368–379. doi: 10.1016/0003-2697(87)90587-2. [DOI] [PubMed] [Google Scholar]
  26. Sugai M., Wu H. C. Export of the outer membrane lipoprotein is defective in secD, secE, and secF mutants of Escherichia coli. J Bacteriol. 1992 Apr;174(8):2511–2516. doi: 10.1128/jb.174.8.2511-2516.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. 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]
  28. Watanabe T., Hayashi S., Wu H. C. Synthesis and export of the outer membrane lipoprotein in Escherichia coli mutants defective in generalized protein export. J Bacteriol. 1988 Sep;170(9):4001–4007. doi: 10.1128/jb.170.9.4001-4007.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Wickner W., Driessen A. J., Hartl F. U. The enzymology of protein translocation across the Escherichia coli plasma membrane. Annu Rev Biochem. 1991;60:101–124. doi: 10.1146/annurev.bi.60.070191.000533. [DOI] [PubMed] [Google Scholar]
  30. 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]

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