Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1982 Apr 1;203(1):33–43. doi: 10.1042/bj2030033

Primary structure of major outer-membrane protein I (ompF protein, porin) of Escherichia coli B/r.

R Chen, C Krämer, W Schmidmayr, U Chen-Schmeisser, U Henning
PMCID: PMC1158189  PMID: 7049161

Abstract

In the outer membrane of Gram-negative bacteria hydrophilic pores exist, allowing the diffusion of various low-molecular-weight solutes. These pores are formed by proteins, the porins. In a preliminary communication [Chen, Krämer, Schmidmayr & Henning (1979) Proc. Natl. Acad. Sci. U.S.A. 76, 5014-5017] we presented the primary structure of one of these porins, the 340-amino-acid-residue protein I (ompF protein) from Escherichia coli B/r. In the present paper we give the experimental evidence for this sequence. Two tryptophan positions, one valine position, two aspartic acid positions and nine out of 82 amide determinations have been corrected. To aid further studies on this class of transmembrane proteins, the isolation of most of the constituent peptides is documented.

Full text

PDF
41

Selected References

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

  1. Benz R., Janko K., Boos W., Läuger P. Formation of large, ion-permeable membrane channels by the matrix protein (porin) of Escherichia coli. Biochim Biophys Acta. 1978 Aug 17;511(3):305–319. doi: 10.1016/0005-2736(78)90269-9. [DOI] [PubMed] [Google Scholar]
  2. Benz R., Janko K., Läuger P. Ionic selectivity of pores formed by the matrix protein (porin) of Escherichia coli. Biochim Biophys Acta. 1979 Mar 8;551(2):238–247. doi: 10.1016/0005-2736(89)90002-3. [DOI] [PubMed] [Google Scholar]
  3. Chang J. Y., Creaser E. H. A novel manual method for protein-sequence analysis. Biochem J. 1976 Jul 1;157(1):77–85. doi: 10.1042/bj1570077. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Chen R., Hindennach I., Henning U. Major proteins of the Escherichia coli outer cell envelope membrane. Sequence of the cyanogen bromide fragments of protein I from Escherichia coli B/r. Hoppe Seylers Z Physiol Chem. 1978 Dec;359(12):1807–1810. [PubMed] [Google Scholar]
  5. Chen R., Krämer C., Schmidmayr W., Henning U. Primary structure of major outer membrane protein I of Escherichia coli B/r. Proc Natl Acad Sci U S A. 1979 Oct;76(10):5014–5017. doi: 10.1073/pnas.76.10.5014. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Chen R., Schmidmayr W., Krämer C., Chen-Schmeisser U., Henning U. Primary structure of major outer membrane protein II (ompA protein) of Escherichia coli K-12. Proc Natl Acad Sci U S A. 1980 Aug;77(8):4592–4596. doi: 10.1073/pnas.77.8.4592. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Chen R. The sequence determination of a protein in a micro scale: the sequence analysis of ribosomal protein L34 of Escherichia coli. Hoppe Seylers Z Physiol Chem. 1976 Jun;357(6):873–886. doi: 10.1515/bchm2.1976.357.1.873. [DOI] [PubMed] [Google Scholar]
  8. Diedrich D. L., Schnaitman C. A. Lysyl-derived aldehydes in outer membrane proteins of Escherichia coli. Proc Natl Acad Sci U S A. 1978 Aug;75(8):3708–3712. doi: 10.1073/pnas.75.8.3708. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. GRAY W. R., HARTLEY B. S. THE STRUCTURE OF A CHYMOTRYPTIC PEPTIDE FROM PSEUDOMONAS CYTOCHROME C-551. Biochem J. 1963 Nov;89:379–380. doi: 10.1042/bj0890379. [DOI] [PubMed] [Google Scholar]
  10. Gamon K., Chen R., Henning U. Major proteins of the outer cell envelope membrane of Escherichia coli K12: multiple species of protein I differ in primary structure. Mol Gen Genet. 1978 Oct 30;166(2):187–192. doi: 10.1007/BF00285921. [DOI] [PubMed] [Google Scholar]
  11. Garavito R. M., Rosenbusch J. P. Three-dimensional crystals of an integral membrane protein: an initial x-ray analysis. J Cell Biol. 1980 Jul;86(1):327–329. doi: 10.1083/jcb.86.1.327. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Garten W., Henning U. Cell envelope and shape of Escherichia coli K12. Isolation and preliminary characterization of the major ghost-membrane proteins. Eur J Biochem. 1974 Sep 1;47(2):343–352. doi: 10.1111/j.1432-1033.1974.tb03699.x. [DOI] [PubMed] [Google Scholar]
  13. Hantke K. Phage T6--colicin K receptor and nucleoside transport in Escherichia coli. FEBS Lett. 1976 Nov;70(1):109–112. doi: 10.1016/0014-5793(76)80737-5. [DOI] [PubMed] [Google Scholar]
  14. Henning U., Schmidmayr W., Hindennach I. Major proteins of the outer cell envelope membrane of Escherichia coli K-12: multiple species of protein I. Mol Gen Genet. 1977 Sep 9;154(3):293–298. doi: 10.1007/BF00571285. [DOI] [PubMed] [Google Scholar]
  15. Henning U., Sonntag I., Hindennach I. Mutants (ompA) affecting a major outer membrane protein of Escherichia coli K12. Eur J Biochem. 1978 Dec;92(2):491–498. doi: 10.1111/j.1432-1033.1978.tb12771.x. [DOI] [PubMed] [Google Scholar]
  16. Heuzenroeder M. W., Reeves P. Periplasmic maltose-binding protein confers specificity on the outer membrane maltose pore of Escherichia coli. J Bacteriol. 1980 Feb;141(2):431–435. doi: 10.1128/jb.141.2.431-435.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Hindennach I., Henning U. The major proteins of the Excherichia coli outer cell envelope membrane. Preparative isolation of all major membrane proteins. Eur J Biochem. 1975 Nov 1;59(1):207–213. doi: 10.1111/j.1432-1033.1975.tb02443.x. [DOI] [PubMed] [Google Scholar]
  18. Ichihara S., Mizushima S. Characterization of major outer membrane proteins O-8 and O-9 of Escherichia coli K-12. Evidence that structural genes for the two proteins are different. J Biochem. 1978 Apr;83(4):1095–1100. doi: 10.1093/oxfordjournals.jbchem.a131998. [DOI] [PubMed] [Google Scholar]
  19. Luckey M., Nikaido H. Diffusion of solutes through channels produced by phage lambda receptor protein of Escherichia coli: inhibition by higher oligosaccharides of maltose series. Biochem Biophys Res Commun. 1980 Mar 13;93(1):166–171. doi: 10.1016/s0006-291x(80)80261-0. [DOI] [PubMed] [Google Scholar]
  20. Nakae T. A porin activity of purified lambda-receptor protein from Escherichia coli in reconstituted vesicle membranes. Biochem Biophys Res Commun. 1979 Jun 13;88(3):774–781. doi: 10.1016/0006-291x(79)91475-x. [DOI] [PubMed] [Google Scholar]
  21. Nakae T. Identification of the outer membrane protein of E. coli that produces transmembrane channels in reconstituted vesicle membranes. Biochem Biophys Res Commun. 1976 Aug 9;71(3):877–884. doi: 10.1016/0006-291x(76)90913-x. [DOI] [PubMed] [Google Scholar]
  22. Nakae T., Ishii J., Tokunaga M. Subunit structure of functional porin oligomers that form permeability channels in the other membrane of Escherichia coli. J Biol Chem. 1979 Mar 10;254(5):1457–1461. [PubMed] [Google Scholar]
  23. Nakamura K., Mizushima S. Effects of heating in dodecyl sulfate solution on the conformation and electrophoretic mobility of isolated major outer membrane proteins from Escherichia coli K-12. J Biochem. 1976 Dec;80(6):1411–1422. doi: 10.1093/oxfordjournals.jbchem.a131414. [DOI] [PubMed] [Google Scholar]
  24. Ozols J., Gerard C. Cleavage of tryptophanyl peptide bonds in cytochrome b5 by cyanogen bromide. J Biol Chem. 1977 Sep 10;252(17):5986–5989. [PubMed] [Google Scholar]
  25. Palva E. T., Randall L. L. Arrangement of protein I in Escherichia coli outer membrane: cross-linking study. J Bacteriol. 1978 Jan;133(1):279–286. doi: 10.1128/jb.133.1.279-286.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Pugsley A. P., Lee D. R., Schnaitman C. A. Genes affecting the major outer membrane proteins of Escherichia coli K-12: mutations at nmpA and nmpB. Mol Gen Genet. 1980;177(4):681–689. doi: 10.1007/BF00272680. [DOI] [PubMed] [Google Scholar]
  27. Pugsley A. P., Schnaitman C. A. Identification of three genes controlling production of new outer membrane pore proteins in Escherichia coli K-12. J Bacteriol. 1978 Sep;135(3):1118–1129. doi: 10.1128/jb.135.3.1118-1129.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Rosenbusch J. P. Characterization of the major envelope protein from Escherichia coli. Regular arrangement on the peptidoglycan and unusual dodecyl sulfate binding. J Biol Chem. 1974 Dec 25;249(24):8019–8029. [PubMed] [Google Scholar]
  29. Schindler H., Rosenbusch J. P. Matrix protein from Escherichia coli outer membranes forms voltage-controlled channels in lipid bilayers. Proc Natl Acad Sci U S A. 1978 Aug;75(8):3751–3755. doi: 10.1073/pnas.75.8.3751. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Steven A. C., Heggeler B., Müller R., Kistler J., Rosenbusch J. P. Ultrastructure of a periodic protein layer in the outer membrane of Escherichia coli. J Cell Biol. 1977 Feb;72(2):292–301. doi: 10.1083/jcb.72.2.292. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Tommassen J., Lugtenberg B. Outer membrane protein e of Escherichia coli K-12 is co-regulated with alkaline phosphatase. J Bacteriol. 1980 Jul;143(1):151–157. doi: 10.1128/jb.143.1.151-157.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Yu F., Ichihara S., Mizushima S. A major outer membrane protein (O-8) of Escherichia coli K-12 exists as a trimer in sodium dodecyl sulfate solution. FEBS Lett. 1979 Apr 1;100(1):71–74. doi: 10.1016/0014-5793(79)81133-3. [DOI] [PubMed] [Google Scholar]
  33. Zalman L. S., Nikaido H., Kagawa Y. Mitochondrial outer membrane contains a protein producing nonspecific diffusion channels. J Biol Chem. 1980 Mar 10;255(5):1771–1774. [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES