Escherichia coli Hsp31 functions as a holding chaperone that cooperates with the DnaK-DnaJ-GrpE system in the management of protein misfolding under severe stress conditions

Molecular Microbiology

Volumn 51, Issue 3, 2004, Pages 849-859

  Mujacic, Mirna ^a   Bader, Martin W ^b   Baneyx, François ^a,c  

^a University of Washington   (United States)

^b UNIVERSITY OF WASHINGTON   (United States)

^c University of Washington   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; CYTOPLASM PROTEIN; GLUCOSE REGULATED PROTEIN; HEAT SHOCK PROTEIN 31; PROTEIN DNAJ; PROTEIN DNAK; PROTEIN HCHA; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL CHROMOSOME; BACTERIAL GENE; BACTERIAL GENETICS; BACTERIAL GROWTH; CELL AGGREGATION; CELL SURVIVAL; CONTROLLED STUDY; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE DELETION; GENE MUTATION; MOLECULAR GENETICS; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FUNCTION; STRESS; TEMPERATURE DEPENDENCE; TEMPERATURE SENSITIVITY; THERMAL ANALYSIS;

BACTERIAL PROTEINS; CELL DIVISION; CELL SURVIVAL; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HEAT; HEAT-SHOCK PROTEINS; HSP40 HEAT-SHOCK PROTEINS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; PROTEIN FOLDING;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 1242297805     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2003.03871.x     Document Type: Article

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