DnaK chaperone-dependent disaggregation by caseinolytic peptidase B (ClpB) mutants reveals functional overlap in the N-terminal domain and nucleotide-binding domain-1 pore tyrosine

Journal of Biological Chemistry

Volumn 287, Issue 34, 2012, Pages 28470-28479

  Doyle, Shannon M ^a   Hoskins, Joel R ^a   Wickner, Sue ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ATPASES; CELLULAR ACTIVITIES; CHAPERONE SYSTEMS; CONFORMATIONAL CHANGE; DISAGGREGATION; DOUBLE MUTANTS; HEXAMERS; MOLECULAR CHAPERONES; N-TERMINAL DOMAINS; OVERLAPPING FUNCTIONS; PROTEIN DISAGGREGATION; SINGLE MUTANT; SUBSTRATE BINDING;

AMINO ACIDS; ESCHERICHIA COLI; NUCLEOTIDES;

SUBSTRATES;

ADENOSINE TRIPHOSPHATE; ALANINE; CASEINOLYTIC PEPTIDASE B; NUCLEOTIDE BINDING PROTEIN; PEPTIDASE; PROTEIN DNAK; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME LOCALIZATION; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; HYDROLYSIS; NUCLEOTIDE BINDING DOMAIN 1; NUCLEOTIDE BINDING DOMAIN 2; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FUNCTION; PROTEIN UNFOLDING;

AMINO ACID SUBSTITUTION; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; MUTATION, MISSENSE; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; TYROSINE;

EID: 84865220378     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.383091     Document Type: Article

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