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PMID: 6291030 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

A prokaryotic membrane anchor sequence: carboxyl terminus of bacteriophage f1 gene III protein retains it in the membrane.

Boeke JD, Model P

Abstract

Gene III protein of bacteriophage f1 is inserted into the host cell membrane where it is assembled into phage particles. A truncated form of gene III protein, encoded by a recombinant plasmid and lacking the carboxyl terminus, does not remain in the membrane but instead appears to slip through it. Fusion of a hydrophobic "membrane anchor" from another membrane protein, the gene VIII protein, to the truncated gene III protein (by manipulation of the recombinant plasmid) restores membrane anchoring. A model for the relationship of gene III protein with the Escherichia coli membrane is discussed.

MeSH Terms
Cell Membrane/physiology Cloning, Molecular Coliphages/genetics DNA Restriction Enzymes Escherichia coli/genetics Genes, Viral Plasmids Viral Proteins/genetics
Chemicals
Viral Proteins DNA Restriction Enzymes
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Boeke J D
Model P
References (26)
26 references, click to expand
  1. Association of newly synthesized major f1 coat protein with infected host cell inner membrane.
    J Supramol Struct. 1972;1(1):8-18 PMID: 4568193
  2. Selective solubilization of proteins and phospholipids from red blood cell membranes by nonionic detergents.
    J Supramol Struct. 1973;1(3):233-48 PMID: 4804838
  3. 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):835-51 PMID: 811671
  4. A simplified representation of protein conformations for rapid simulation of protein folding.
    J Mol Biol. 1976 Jun 14;104(1):59-107 PMID: 957439
  5. Rat insulin genes: construction of plasmids containing the coding sequences.
    Science. 1977 Jun 17;196(4296):1313-9 PMID: 325648
  6. Adsorption protein of the bacteriophage fd: isolation, molecular properties, and location in the virus.
    Biochemistry. 1977 Jun 14;16(12):2686-94 PMID: 329863
  7. 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):361-5 PMID: 343108
  8. 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):8667-70 PMID: 214427
  9. 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):1251-5 PMID: 375232
  10. Use of gene fusion to study secretion of maltose-binding protein into Escherichia coli periplasm.
    J Bacteriol. 1979 Jul;139(1):19-31 PMID: 110778
  11. Translocation of proteins across membranes: the signal hypothesis and beyond.
    Symp Soc Exp Biol. 1979;33:9-36 PMID: 524275
  12. Two mRNAs with different 3' ends encode membrane-bound and secreted forms of immunoglobulin mu chain.
    Cell. 1980 Jun;20(2):303-12 PMID: 6771019
  13. A mechanism of protein localization: the signal hypothesis and bacteria.
    J Cell Biol. 1980 Sep;86(3):701-11 PMID: 6447703
  14. 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):4669-73 PMID: 7001463
  15. Replication of bacteriophage f1: a complex containing gene II protein in gene V mutant-infected bacteria.
    J Mol Biol. 1980 May 25;139(3):393-405 PMID: 7441740
  16. Limited proteolysis of the penicillin-sensitive D-alanine carboxypeptidase purified from Bacillus subtilis membranes. Active water-soluble fragments generated by cleavage of a COOH-terminal membrane anchor.
    J Biol Chem. 1981 Feb 25;256(4):2059-66 PMID: 6780558
  17. Primary structure of the COOH-terminal membranous segment of a penicillin-sensitive enzyme purified from two Bacilli.
    J Biol Chem. 1981 Feb 25;256(4):2067-77 PMID: 6780559
  18. 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):103-16 PMID: 7230262
  19. Protein localization in E. coli: is there a common step in the secretion of periplasmic and outer-membrane proteins?
    Cell. 1981 Jun;24(3):707-17 PMID: 6788377
  20. Adsorption complex of filamentous fd virus.
    J Mol Biol. 1981 Mar 15;146(4):621-7 PMID: 7024557
  21. Precursor forms of penicillin-binding proteins 5 and 6 of E. coli cytoplasmic membrane.
    Nature. 1981 Sep 24;293(5830):307-9 PMID: 7024823
  22. E. coli mutant pleiotropically defective in the export of secreted proteins.
    Cell. 1981 Sep;25(3):765-72 PMID: 7026050
  23. The "steady state" of coliphage f1: DNA synthesis late in infection.
    Virology. 1981 Dec;115(2):282-94 PMID: 7032054
  24. Domain structure of bacteriophage fd adsorption protein.
    FEBS Lett. 1981 Nov 30;135(1):167-72 PMID: 7032968
  25. Structure of genes for membrane and secreted murine IgD heavy chains.
    Nature. 1982 Apr 1;296(5856):410-5 PMID: 6801528
  26. Filamentous phage pre-coat is an integral membrane protein: analysis by a new method of membrane preparation.
    Cell. 1982 Jan;28(1):177-84 PMID: 7066983
Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1982-09-00
Pages
5200-4
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC346863
Subset
IM
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