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Requires the exposure of 32 sites to bind DnaJ. Significance: This model can be applied to chaperone action in helping newly synthesized polypeptides to fold. Escherichia coli heat shock transcription factor 32 is rapidly degraded by ATP-dependent proteases, such as FtsH and ClpYQ. Although the DnaK chaperone system (DnaK, DnaJ, and GrpE) promotes 32 degradation in vivo, the precise mechanism that
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70 chaperone system consists of Hsp70, Hsp40, and a nucleotide exchange factor (Hsp70 has an ATPase activity). Although the ATP-bound form of Hsp70 has a low affinity for substrates due to its high substrate exchange rate, the ADP-bound form has a higher affinity for substrates with a low substrate exchange rate. Hsp40 acts as a co-chaperone and activates the Hsp70 ATPase, although it also acts as
IONS FOR HEAT SHOCK PROTEIN 70 (Hsp70)-Hsp40 MODE OF FUNCTIONSReceived for publication, December 7, 2011, and in revised form, April 9, 2012 Published, JBC Papers in Press, April 10, 2012, DOI 10.1074/jbc.M111.Hirotaka Suzuki, Ayami Ikeda, Sachie Tsuchimoto, Ko-ichi Adachi, Aki Noguchi, Yoshihiro Fukumori, and Masaaki Kanemori1 From the School of Natural System, College of Science and Engineering,
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