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. 1976 Apr;73(4):1159–1163. doi: 10.1073/pnas.73.4.1159

Asymmetric orientation of phage M13 coat protein in Escherichia coli cytoplasmic membranes and in synthetic lipid vesicles.

W Wickner
PMCID: PMC430220  PMID: 772680

Abstract

At each stage of infection, the major coat protein of coliphage M13 binds to the E. coli cytoplasmic membrane with its antigenic site exposed to the cell exterior [Wickner, W. (1975) Proc. Nat. Acad. Sci. USA 72, 4749-4753]. This antigenic site is now shown to be at the amino-terminus of the protein. The amino-terminus of M13 coat protein is also found exclusively on the outside of dilauroyl or dimyristoyl lecithin vesicles, formed with coat protein by the cholate dilution technique [Racker, E., et al. (1975) FEBS Lett. 57, 14-18] near the lipid phase transition temperature. The basic carboxyterminus of the coat protein is exclusively on the inside of these vesicles. Vesicles of M13 coat protein and dimyristoyl lecithin when formed below the lipid phase transition temperature have both ends of the coat protein exposed to the vesicle exterior. The asymmetry of a membrane protein can, therefore, be established in the absence of other proteins and of lipid asymmetry; it depends on the physical state of the lipid phase. The factors which cause asymmetry in this model system may affect the distribution of proteins in biological membranes.

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Selected References

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

  1. Asbeck F., Beyreuther K., Köhler H., von Wettstein G., Braunitzer G. Virusproteine, IV. Die Konstitution des Hüllproteins des Phagen fd. Hoppe Seylers Z Physiol Chem. 1969 Sep;350(9):1047–1066. [PubMed] [Google Scholar]
  2. Knippers R., Hoffmann-Berling H. A coat protein from bacteriophage fd. I. Hydrodynamic measurements and biological characterization. J Mol Biol. 1966 Nov 14;21(2):281–292. doi: 10.1016/0022-2836(66)90099-4. [DOI] [PubMed] [Google Scholar]
  3. Linden C. D., Wright K. L., McConnell H. M., Fox C. F. Lateral phase separations in membrane lipids and the mechanism of sugar transport in Escherichia coli. Proc Natl Acad Sci U S A. 1973 Aug;70(8):2271–2275. doi: 10.1073/pnas.70.8.2271. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Marco R., Jazwinski S. M., Kornberg A. Binding, eclipse, and penetration of the filamentous bacteriophage M13 in intact and disrupted cells. Virology. 1974 Nov;62(1):209–223. doi: 10.1016/0042-6822(74)90316-x. [DOI] [PubMed] [Google Scholar]
  5. Marvin D. A., Hohn B. Filamentous bacterial viruses. Bacteriol Rev. 1969 Jun;33(2):172–209. doi: 10.1128/br.33.2.172-209.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Marvin D. A., Wachtel E. J. Structure and assembly of filamentous bacterial viruses. Nature. 1975 Jan 3;253(5486):19–23. doi: 10.1038/253019a0. [DOI] [PubMed] [Google Scholar]
  7. Nakashima Y., Konigsberg W. Reinvestigation of a region of the fd bacteriophage coat protein sequence. J Mol Biol. 1974 Sep 25;88(3):598–600. doi: 10.1016/0022-2836(74)90410-0. [DOI] [PubMed] [Google Scholar]
  8. Racker E., Chien T. F., Kandrach A. A cholate-dilution procedure for the reconstitution of the Ca++ pump, 32Pi--ATP exchange, and oxidative phosphorylation. FEBS Lett. 1975 Sep 1;57(1):14–18. doi: 10.1016/0014-5793(75)80141-4. [DOI] [PubMed] [Google Scholar]
  9. Singer S. J. The molecular organization of membranes. Annu Rev Biochem. 1974;43(0):805–833. doi: 10.1146/annurev.bi.43.070174.004105. [DOI] [PubMed] [Google Scholar]
  10. Smilowitz H. Bacteriophage f1 infection: fate of the parental major coat protein. J Virol. 1974 Jan;13(1):94–99. doi: 10.1128/jvi.13.1.94-99.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Smilowitz H., Carson J., Robbins P. W. Association of newly synthesized major f1 coat protein with infected host cell inner membrane. J Supramol Struct. 1972;1(1):8–18. doi: 10.1002/jss.400010103. [DOI] [PubMed] [Google Scholar]
  12. Trenkner E., Bonhoeffer F., Gierer A. The fate of the protein component of bacteriophage fd during infection. Biochem Biophys Res Commun. 1967 Sep 27;28(6):932–939. doi: 10.1016/0006-291x(67)90069-1. [DOI] [PubMed] [Google Scholar]
  13. Wickner W. Asymmetric orientation of a phage coat protein in cytoplasmic membrane of Escherichia coli. Proc Natl Acad Sci U S A. 1975 Dec;72(12):4749–4753. doi: 10.1073/pnas.72.12.4749. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Woolford J. L., Jr, Webster R. E. Proteolytic digestion of the micellar complex of f1 coat protein and deoxycholate. J Biol Chem. 1975 Jun 10;250(11):4333–4339. [PubMed] [Google Scholar]

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