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.
journal_name
Proc Natl Acad Sci U S Aauthors
Horiuchi S,Tai PC,Davis BDdoi
10.1073/pnas.80.11.3287subject
Has Abstractpub_date
1983-06-01 00:00:00pages
3287-91issue
11eissn
0027-8424issn
1091-6490journal_volume
80pub_type
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