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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
. 1985 Dec;82(23):7955–7959. doi: 10.1073/pnas.82.23.7955

Binding of pea cytochrome f to the inner membrane of Escherichia coli requires the bacterial secA gene product.

S J Rothstein, A A Gatenby, D L Willey, J C Gray
PMCID: PMC390889  PMID: 2999786

Abstract

Various sequences from the 5' end of the pea chloroplast gene for cytochrome f have been fused in the correct reading frame with lacZ, and the cellular location of the hybrid polypeptides in Escherichia coli has been examined. Hybrid polypeptides containing N-terminal parts of cytochrome f are located in the cytoplasmic membrane of E. coli. Membrane localization is most efficient when the intact signal sequence of cytochrome f is present at the N-terminal end of the fusion proteins. Fusion within the signal sequence, so that the processing site is absent, reduces the efficiency of membrane binding. Membrane insertion of fusion proteins containing signal sequences is prevented in a temperature-sensitive secA strain at the nonpermissive temperature and the hybrid proteins accumulate in the cytoplasm. This indicates that specific recognition of the chloroplast signal sequence occurs in the bacterial secretory pathway.

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Selected References

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