A single ClpS monomer is sufficient to direct the activity of the ClpA hexamer

Journal of Biological Chemistry

Volumn 285, Issue 12, 2010, Pages 8771-8781

  De Donatis, Gian Marco ^a   Singh, Satyendra K ^a   Viswanathan, Sarada ^a   Maurizi, Michael R ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEINS; AXIAL CHANNEL; HEXAMERS; HIGH AFFINITY; SUBSTRATE BINDING;

BINDING ENERGY; BINDING SITES; BIOCHEMISTRY; DEGRADATION; DYES; MOLECULES; PROTEINS;

SUBSTRATES;

ADAPTOR PROTEIN; ESCHERICHIA COLI PROTEIN; MONOMER; PROTEIN CLPA; PROTEIN CLPS; UNCLASSIFIED DRUG; CARRIER PROTEIN; CHAPERONIN; CLPA PROTEASE, E COLI; CLPS PROTEIN, E COLI; ENDOPEPTIDASE CLP; PEPTIDE HYDROLASE;

ARTICLE; BINDING AFFINITY; BINDING COMPETITION; BINDING SITE; COMPLEX FORMATION; CONTROLLED STUDY; HALF LIFE TIME; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; TEMPERATURE SENSITIVITY; CHEMISTRY; DOSE RESPONSE; ENZYMOLOGY; ESCHERICHIA COLI; GENE EXPRESSION REGULATION; KINETICS; METABOLISM; PHYSIOLOGY; PLASMID; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; TIME;

CARRIER PROTEINS; CHAPERONINS; DOSE-RESPONSE RELATIONSHIP, DRUG; ENDOPEPTIDASE CLP; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENE EXPRESSION REGULATION, BACTERIAL; KINETICS; PEPTIDE HYDROLASES; PLASMIDS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN INTERACTION MAPPING; TIME FACTORS;

EID: 77950578789     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.053736     Document Type: Article

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