Nucleotide binding by Lhs1p is essential for its nucleotide exchange activity and for function in Vivo

Journal of Biological Chemistry

Volumn 284, Issue 46, 2009, Pages 31564-31571

  de Keyzer, Jeanine ^a   Steel, Gregor J ^a   Hale, Sarah J ^a   Humphries, Daniel ^a   Stirling, Colin J ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ATP BINDING; ATP HYDROLYSIS; DOMAIN STRUCTURE; ENDOPLASMIC RETICULUM; HSP70 CHAPERONES; IN-VITRO; IN-VIVO; N-TERMINALS; NUCLEOTIDE BINDING; NUCLEOTIDE EXCHANGE; NUCLEOTIDE-BINDING DOMAIN; NUCLEOTIDE-EXCHANGE FACTOR; PROTEIN AGGREGATION; PROTEIN TRANSLOCATION; SACCHAROMYCES CEREVISIAE; SUBSTRATE BINDING; SUBSTRATE BINDING DOMAIN;

PROTEIN FOLDING;

NUCLEOTIDES;

ADENOSINE TRIPHOSPHATE; CHAPERONE; COCHAPERONE; ENZYME; HEAT SHOCK PROTEIN 70; HOLDASE; NUCLEOTIDE; NUCLEOTIDE EXCHANGE FACTOR; PROTEIN KAR2P; PROTEIN LHS1P; PROTEIN SIL1P; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME SUBSTRATE; GENE MUTATION; GENE TRANSLOCATION; HYDROLYSIS; IN VITRO STUDY; IN VIVO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN TRANSPORT;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; ENDOPLASMIC RETICULUM; FUNGAL PROTEINS; HSP70 HEAT-SHOCK PROTEINS; HYDROLYSIS; LUCIFERASES; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN FOLDING; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

SACCHAROMYCES CEREVISIAE;

EID: 70450245119     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.055160     Document Type: Article

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