Document Detail

The isolated proteolytic domain of Escherichia coli ATP-dependent protease Lon exhibits the peptidase activity.
MedLine Citation:
PMID:  9720920     Owner:  NLM     Status:  MEDLINE    
Selective protein degradation is an energy-dependent process performed by high-molecular-weight proteases. The activity of proteolytic components of these enzymes is coupled to the ATPase activity of their regulatory subunits or domains. Here, we obtained the proteolytic domain of Escherichia coli protease Lon by cloning the corresponding fragment of the lon gene in pGEX-KG, expression of the hybrid protein, and isolation of the proteolytic domain after hydrolysis of the hybrid protein with thrombin. The isolated proteolytic domain exhibited almost no activity toward protein substrates (casein) but hydrolyzed peptide substrates (melittin), thereby confirming the importance of the ATPase component for protein hydrolysis. Protease Lon and its proteolytic domain differed in the efficiency and specificity of melittin hydrolysis.
F S Rasulova; N I Dergousova; N N Starkova; E E Melnikov; L D Rumsh; L M Ginodman; T V Rotanova
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  FEBS letters     Volume:  432     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  1998 Aug 
Date Detail:
Created Date:  1998-09-18     Completed Date:  1998-09-18     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  179-81     Citation Subset:  IM    
Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow.
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MeSH Terms
ATP-Dependent Proteases
Amino Acid Sequence
Endopeptidases / metabolism*
Escherichia coli / chemistry,  enzymology*
Escherichia coli Proteins*
Heat-Shock Proteins / chemistry*,  isolation & purification,  metabolism*
Melitten / metabolism
Molecular Sequence Data
Protease La*
Protein Structure, Tertiary
Serine Endopeptidases / chemistry*,  isolation & purification,  metabolism*
Reg. No./Substance:
0/Escherichia coli Proteins; 0/Heat-Shock Proteins; 20449-79-0/Melitten; EC 3.4.-/Endopeptidases; EC 3.4.21.-/ATP-Dependent Proteases; EC 3.4.21.-/Serine Endopeptidases; EC protein, E coli; EC La

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