The CtsR regulator of stress response is active as a dimer and specifically degraded in vivo at 37°c

Molecular Microbiology

Volumn 38, Issue 2, 2000, Pages 335-347

  Derre, I ^a   Rapoport, G ^a   Msadek, T ^a  

^a INSTITUT PASTEUR   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CLASS THREE STRESS GENE REPRESSOR; DIMER; DNA BINDING PROTEIN; HEAT SHOCK PROTEIN; HELIX LOOP HELIX PROTEIN; HYBRID PROTEIN; PROTEINASE; REPRESSOR PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; DIMERIZATION; GENE EXPRESSION REGULATION; GRAM POSITIVE BACTERIUM; HEAT SHOCK; IN VITRO STUDY; IN VIVO STUDY; MUTAGENESIS; NONHUMAN; OPERATOR GENE; OPERON; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DNA BINDING; PROTEIN EXPRESSION; STRUCTURE ACTIVITY RELATION; TEMPERATURE; WESTERN BLOTTING;

ADENOSINE TRIPHOSPHATASES; AMINO ACID SEQUENCE; BACILLUS SUBTILIS; BACTERIAL PROTEINS; DIMERIZATION; DNA; ENDOPEPTIDASE CLP; ESCHERICHIA COLI PROTEINS; GENES, BACTERIAL; GLYCINE; HEAT-SHOCK PROTEINS; HELIX-TURN-HELIX MOTIFS; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; MUTAGENESIS; PROTEIN STRUCTURE, TERTIARY; REPRESSOR PROTEINS; SERINE ENDOPEPTIDASES; TEMPERATURE;

FIRMICUTES; POSIBACTERIA;

EID: 0033735885     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2000.02124.x     Document Type: Article

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