Mutations in the interdomain linker region of DnaK abolish the chaperone action of the DnaK/DnaJ/GrpE system

FEBS Letters

Volumn 497, Issue 1, 2001, Pages 55-58

  Han, Wanjiang ^a   Christen, Philipp ^a  

^a UNIVERSITY OF ZURICH   (Switzerland)

Author keywords

DnaJ; DnaK; Hsp40; Hsp70; Molecular chaperone; Oligomerization

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CHAPERONE; LEUCINE; LUCIFERASE; PROTEIN DNAJ; PROTEIN DNAK; PROTEIN GRPE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; ENZYME ACTIVITY; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN FOLDING;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; CONSERVED SEQUENCE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; FLUORESCENT DYES; HEAT-SHOCK PROTEINS; HSP40 HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; MOLECULAR CHAPERONES; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY;

ESCHERICHIA COLI;

EID: 0035907104     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(01)02435-8     Document Type: Article

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