Document Detail


Molecular determinants of MecA as a degradation tag for the ClpCP protease.
MedLine Citation:
PMID:  19767395     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Regulated proteolysis by ATP-dependent proteases is universal in all living cells. In Bacillus subtilis, the degradation of the competence transcription factor ComK is mediated by a ternary complex involving the adaptor protein MecA and the ATP-dependent protease ClpCP. Here we demonstrate that a C-terminal, 98-amino acid domain of MecA (residues 121-218) serves as a non-recycling, degradation tag and targets a variety of fusion proteins to the ClpCP protease for degradation. MecA-(121-218) facilitates productive oligomerization of ClpC, stimulates the ATPase activity of ClpC, and allows the activated ClpC complex to stably associate with ClpP. Importantly, the ClpCP protease undergoes dynamic cycles of assembly and disassembly, which are triggered by association with MecA and the degradation of MecA, respectively.
Authors:
Ziqing Mei; Feng Wang; Yutao Qi; Zhiyuan Zhou; Qi Hu; Han Li; Jiawei Wu; Yigong Shi
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-09-18
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  284     ISSN:  1083-351X     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2009 Dec 
Date Detail:
Created Date:  2009-11-30     Completed Date:  2009-12-22     Revised Date:  2013-05-31    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  34366-75     Citation Subset:  IM    
Affiliation:
Ministry of Education Protein Science Laboratory, Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphatases / chemistry
Amino Acids / chemistry
Bacillus subtilis / metabolism*
Bacterial Proteins / chemistry,  metabolism*
Cloning, Molecular
Endopeptidase Clp / chemistry,  metabolism,  physiology*
Endopeptidases / chemistry
Gene Expression Regulation, Bacterial
Heat-Shock Proteins / chemistry,  metabolism*
Models, Biological
Peptide Hydrolases / metabolism*
Polymerase Chain Reaction
Protein Folding
Protein Structure, Tertiary
Recombinant Fusion Proteins / chemistry
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Bacterial Proteins; 0/ClpC protein, Bacteria; 0/Heat-Shock Proteins; 0/Recombinant Fusion Proteins; 0/mecA protein, Bacillus subtilis; EC 3.4.-/Endopeptidases; EC 3.4.-/Peptide Hydrolases; EC 3.4.21.92/Endopeptidase Clp; EC 3.6.1.-/Adenosine Triphosphatases
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