Functional Domains of the ClpA and ClpX Molecular Chaperones Identified by Limited Proteolysis and Deletion Analysis

Journal of Biological Chemistry

Volumn 276, Issue 31, 2001, Pages 29420-29429

  Singh, Satyendra K ^a   Rozycki, Jan ^a   Ortega, Joaquin ^b   Ishikawa, Takashi ^b   Lo, John ^c   Steven, Alasdair C ^b   Maurizi, Michael R ^a,b  

^a NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES   (United States)

^b NATIONAL CANCER INSTITUTE   (United States)

^c MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; BINDING ENERGY; ESCHERICHIA COLI; SUBSTRATES;

FUNCTIONAL DOMAINS; PROTEOLYSIS;

BIOCHEMISTRY;

ADENOSINE TRIPHOSPHATASE; AMINO ACID; CHAPERONE; CLPA ENZYME; CLPX ENZYME; ENZYME; HOLOENZYME; PROTEINASE; UNCLASSIFIED DRUG; ADENOSINE 5' O (3 THIOTRIPHOSPHATE); ADENOSINE 5'-O-(3-THIOTRIPHOSPHATE); ADENOSINE TRIPHOSPHATE; CLPA PROTEASE, E COLI; CLPX PROTEIN, E COLI; DRUG DERIVATIVE; ENDOPEPTIDASE CLP; ESCHERICHIA COLI PROTEIN; LYSYL ENDOPEPTIDASE; PRIMER DNA; RECOMBINANT PROTEIN; SERINE PROTEINASE;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; ESCHERICHIA COLI; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN INTERACTION; AMINO ACID SEQUENCE; CHEMISTRY; ELECTRON MICROSCOPY; ENZYME SPECIFICITY; GENE DELETION; GENETICS; KINETICS; MACROMOLECULE; METABOLISM; MOLECULAR GENETICS; MUTAGENESIS; NUCLEOTIDE SEQUENCE; ULTRASTRUCTURE;

ESCHERICHIA COLI;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; BASE SEQUENCE; BINDING SITES; CONSERVED SEQUENCE; DNA PRIMERS; ENDOPEPTIDASE CLP; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; KINETICS; MACROMOLECULAR SUBSTANCES; MICROSCOPY, ELECTRON; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; MUTAGENESIS; RECOMBINANT PROTEINS; SEQUENCE DELETION; SERINE ENDOPEPTIDASES; SUBSTRATE SPECIFICITY;

EID: 0035800729     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M103489200     Document Type: Article

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