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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1980 Aug;77(8):4669–4673. doi: 10.1073/pnas.77.8.4669

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

T Date, J M Goodman, W T Wickner
PMCID: PMC349907  PMID: 7001463

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.

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Selected References

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