Physical interaction between bacterial heat shock protein (Hsp) 90 and Hsp70 chaperones mediates their cooperative action to refold denatured proteins

Journal of Biological Chemistry

Volumn 289, Issue 9, 2014, Pages 6110-6119

  Nakamoto, ^a   Fujita, Kensaku ^a   Ohtaki, Aguru ^a   Watanabe, Satoru ^b   Narumi, Shoichi ^a   Maruyama, Takahiro ^a   Suenaga, Emi ^c   Misono, Tomoko S ^c   Kumar, Penmetcha K R ^c   Goloubinoff, Pierre ^d   Yoshikawa, Hirofumi ^e  

^a SAITAMA UNIVERSITY   (Japan)

^b TOKYO UNIVERSITY OF AGRICULTURE   (Japan)

^c NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

^d UNIVERSITY OF LAUSANNE   (Switzerland)

^e JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOSE-6-PHOSPHATE DEHYDROGENASE; HEAT-SHOCK PROTEIN 90; IMMUNOPRECIPITATION ASSAYS; LACTATE DEHYDROGENASE; MALATE DEHYDROGENASE; MOLECULAR CHAPERONES; PHYSICAL INTERACTIONS; SUB-MICROMOLAR AFFINITY;

DENATURATION; SUBSTRATES; UREA;

PROTEINS;

ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; CHAPERONE; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; HIGH TEMPERATURE PROTEIN G; LACTATE DEHYDROGENASE; MALATE DEHYDROGENASE; PROTEIN DNAJ; PROTEIN DNAJ2; PROTEIN DNAK; PROTEIN DNAK2; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; CYANOBACTERIUM; ESCHERICHIA COLI; IMMUNOPRECIPITATION; IN VITRO STUDY; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN HYDROLYSIS; PROTEIN PROTEIN INTERACTION; SURFACE PLASMON RESONANCE;

CYANOBACTERIA; DNAJ; DNAK; HEAT SHOCK PROTEIN; HSP70; HSP90; HTPG; MOLECULAR CHAPERONE; PROTEIN AGGREGATION;

ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEINS; GLUCOSEPHOSPHATE DEHYDROGENASE; HSP70 HEAT-SHOCK PROTEINS; HSP90 HEAT-SHOCK PROTEINS; PROTEIN DENATURATION; PROTEIN FOLDING; SYNECHOCOCCUS; UREA;

EID: 84896846203     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.524801     Document Type: Article

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