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PMID: 1740190 Published · ppublish English Journal Article Review

Proteases and protein degradation in Escherichia coli.

Experientia ·Vol. 48 ·No. 2 ·1992-02-15 ·Pages 178-201

Maurizi MR

Abstract

In E. coli, protein degradation plays important roles in regulating the levels of specific proteins and in eliminating damaged or abnormal proteins. E. coli possess a very large number of proteolytic enzymes distributed in the cytoplasm, the inner membrane, and the periplasm, but, with few exceptions, the physiological functions of these proteases are not known. More than 90% of the protein degradation occurring in the cytoplasm is energy-dependent, but the activities of most E. coli proteases in vitro are not energy-dependent. Two ATP-dependent proteases, Lon and Clp, are responsible for 70-80% of the energy-dependent degradation of proteins in vivo. In vitro studies with Lon and Clp indicate that both proteases directly interact with substrates for degradation. ATP functions as an allosteric effector promoting an active conformation of the proteases, and ATP hydrolysis is required for rapid catalytic turnover of peptide bond cleavage in proteins. Lon and Clp show virtually no homology at the amino acid level, and thus it appears that at least two families of ATP-dependent proteases have evolved independently.

MeSH Terms
Bacterial Proteins/metabolism Endopeptidases/metabolism Escherichia coli/enzymology Models, Biological Proteins/metabolism Substrate Specificity
Chemicals
Bacterial Proteins Proteins Endopeptidases
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Maurizi M R
Laboratory of Cell Biology, National Cancer Institute, Bethesda, Maryland 20892.
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Article Info
Journal
Experientia
Abbr.
Experientia
ISSN
0014-4754
DOI
10.1007/BF01923511
Published
1992-02-15
Pages
178-201
Language
English
Region
Switzerland
NLM ID
0376547
Subset
IM
External Links
PubMed source DOI: 10.1007/BF01923511
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