Procoat, the precursor of M13 coat protein, requires an electrochemical potential for membrane insertion.

T. Date, J. M. Goodman, W. T. Wickner

Research output: Contribution to journalArticle

93 Citations (Scopus)

Abstract

The coat protein of coliphage M13 spans the host cell cytoplasmic membrane prior to its assembly into extruding virus. It is made as a soluble cytoplasmic precursor, termed "procoat," with 23 extra amino acid residues at the NH2 terminus. Procoat binds to the cell membrane and is converted proteolytically to coat protein. When the electrochemical gradient of an infected cell is rapidly dissipated by uncouplers, procoat still binds to the plasma membrane but is not converted to coat. We report here that membrane-bound procoat is only detected at the inner face of the cytoplasmic membrane and that uncouplers prevent it from integrating into a transmembrane conformation.

Original languageEnglish (US)
Pages (from-to)4669-4673
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume77
Issue number8
StatePublished - Aug 1980

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Capsid Proteins
Membrane Potentials
Cell Membrane
Bacteriophage M13
Viruses
Amino Acids
Membranes

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

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AB - The coat protein of coliphage M13 spans the host cell cytoplasmic membrane prior to its assembly into extruding virus. It is made as a soluble cytoplasmic precursor, termed "procoat," with 23 extra amino acid residues at the NH2 terminus. Procoat binds to the cell membrane and is converted proteolytically to coat protein. When the electrochemical gradient of an infected cell is rapidly dissipated by uncouplers, procoat still binds to the plasma membrane but is not converted to coat. We report here that membrane-bound procoat is only detected at the inner face of the cytoplasmic membrane and that uncouplers prevent it from integrating into a transmembrane conformation.

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