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. 1983 Jun;80(11):3287–3291. doi: 10.1073/pnas.80.11.3287

A 64-kilodalton membrane protein of Bacillus subtilis covered by secreting ribosomes.

S Horiuchi, P C Tai, B D Davis
PMCID: PMC394026  PMID: 6407010

Abstract

The complexed (ribosome-bearing) membrane fraction of Bacillus subtilis contains several proteins (CM-proteins) that are virtually absent from the ribosome-free fraction and hence might be components of the apparatus of protein secretion. We have determined, by trypsin digestion and by labeling with a nonpenetrating reagent (diazoiodosulfanilic acid), the accessibility of four of these proteins on the two surfaces of the membrane, as exposed either in protoplasts or in inverted membrane vesicles. The 68-kilodalton protein is a transmembrane protein and the 45-kilodalton protein faces only the external surface, whereas the 31-kilodalton protein is inaccessible from either side. Of particular interest is the 64-kilodalton protein: it can be digested by trypsin, and can bind antibody, on the cytoplasmic surface, but only after the ribosomes have been released. This protein is thus evidently a component of the apparatus of protein secretion, closely covered by secreting ribosomes. Whether the other CM-proteins are also involved in protein secretion is uncertain.

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

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