Abstract:
:Studies of the mechanism of protein secretion in a Gram-positive bacterium, Bacillus subtilis, yielded results very similar to those previously obtained with a Gram-negative organism: nascent chains protruding from protoplasts could be labeled extracellularly; the labeled chains could be recovered on polysomes isolated from the membrane--polysome fraction; they could be released by puromycin, low Mg2+, or chain completion; the completed chains include a known secreted protein (alpha-amylase); and their ribosomes appear to be attached to membrane solely by their nascent chains. The reagent used for extracellular labeling, [1252]diazoiodosulfanilic acid, yielded severalfold more specific labeling of the nascent chains (7--10% of the total cellular labeling and one-fourth to one-third of that of the membrane--polysome fraction) than was obtained earlier with another nonpenetrating reagent.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Smith WP,Tai PC,Davis BDdoi
10.1021/bi00568a030subject
Has Abstractpub_date
1979-01-09 00:00:00pages
198-202issue
1eissn
0006-2960issn
1520-4995journal_volume
18pub_type
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