Document Detail


On the relationship between the metabolic and thermodynamic stabilities of T4 lysozymes. Measurements in Escherichia coli.
MedLine Citation:
PMID:  7961892     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Escherichia coli cells were transformed with plasmids encoding 12 site-specific variants of T4 lysozyme, and pulse-chase protocols were used to measure the metabolic stability of each protein. The resulting half-lives ranged from 1 h to more than 50 h. Although the metabolic half-lives of T4 lysozymes correlated roughly with their thermal stabilities, three mutant enzymes were clear exceptions. A reasonably temperature-resistant variant, G156D, exhibited a half-life of 1 h. By contrast, two temperature-sensitive variants, T157I and I3G, were as metabolically stable as wild-type T4 lysozyme. Degradation of two short lived variants, L91P and G156P, required ATP both in vivo and in vitro. Degradation of variant and wild-type enzymes was unimpaired in cells lacking the Lon protease, Clp A or Clp P. However, degradation of L91P and G156D was inhibited in Clp B-cells. Decreased proteolysis of L91P was accompanied by its accumulation in inclusion bodies, indicating that Clp B prevents accumulation of aggregated protein either by preventing aggregation of misfolded polypeptides or solubilizing aggregates.
Authors:
I Inoue; M Rechsteiner
Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  269     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1994 Nov 
Date Detail:
Created Date:  1994-12-19     Completed Date:  1994-12-19     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  29241-6     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, University of Utah School of Medicine, Salt Lake City 84132.
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphate / metabolism
Bacteriophage T4 / enzymology*
Endopeptidases / metabolism
Enzyme Stability
Escherichia coli / enzymology,  genetics*,  virology
Inclusion Bodies
Muramidase / chemistry,  genetics,  metabolism*
Temperature
Thermodynamics
Grant Support
ID/Acronym/Agency:
GM-27159/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
56-65-5/Adenosine Triphosphate; EC 3.2.1.17/Muramidase; EC 3.4.-/Endopeptidases

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