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PMID: 3520569 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Secretion of beta-lactamase into the periplasm of Escherichia coli: evidence for a distinct release step associated with a conformational change.

Minsky A, Summers RG, Knowles JR

Abstract

The secretion of beta-lactamase (EC 3.5.2.6) into the periplasm of Escherichia coli has been followed by pulse-chase labeling at 15 degrees C. Though the periplasmic fraction contains only the mature form of the enzyme, the spheroplast fraction contains the completed precursor and a hitherto undocumented processed form. When whole spheroplasts are treated with trypsin, the processed form in this fraction is completely digested. This is in contrast to the native mature enzyme localized in the periplasm, which is trypsin resistant. The beta-lactamase is evidently processed after translocation to a trypsin-sensitive form that is transiently bound to the periplasmic face of the inner membrane. The release of this processed form into the periplasm occurs concomitantly with a conformational change that results in the soluble, catalytically active, trypsin-resistant structure.

MeSH Terms
Cell Compartmentation Cell Membrane/enzymology Escherichia coli/enzymology Protein Conformation Time Factors Trypsin beta-Lactamases/biosynthesis,metabolism
Chemicals
Trypsin beta-Lactamases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Minsky A
Summers R G
Knowles J R
References (23)
23 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1986-06-00
Pages
4180-4
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC323695
Subset
IM
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