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Chequeball93

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Tive substrate, bacteriophage P1 RepA protein, have located DnaK- and DnaJ-binding sites in RepA (25). To gain further insight into chaperone functions in 32 degradation, we isolated many 32 mutants that are stable in vivo (26). These mutants contain one or two amino acid substitutions in the N-terminal half of Region 2.1. In this study, we examined the affinity of some mutant 32 for proteases and
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Ases its substrates. After dissociation from Hsp70, the polypeptide chains fold into a functional three-dimensional architecture. A model has been proposed in which Hsp40 first recognizes and binds substrate polypeptides and then transfers them to Hsp70. However, in some cases, DnaK itself recognizes and binds to substrate polypeptides independent of DnaJ, as in the case of 32 (24). Because most o
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Ases its substrates. After dissociation from Hsp70, the polypeptide chains fold into a functional three-dimensional architecture. A model has been proposed in which Hsp40 first recognizes and binds substrate polypeptides and then transfers them to Hsp70. However, in some cases, DnaK itself recognizes and binds to substrate polypeptides independent of DnaJ, as in the case of 32 (24). Because most o
1
Ases its substrates. After dissociation from Hsp70, the polypeptide chains fold into a functional three-dimensional architecture. A model has been proposed in which Hsp40 first recognizes and binds substrate polypeptides and then transfers them to Hsp70. However, in some cases, DnaK itself recognizes and binds to substrate polypeptides independent of DnaJ, as in the case of 32 (24). Because most o
1
Ases its substrates. After dissociation from Hsp70, the polypeptide chains fold into a functional three-dimensional architecture. A model has been proposed in which Hsp40 first recognizes and binds substrate polypeptides and then transfers them to Hsp70. However, in some cases, DnaK itself recognizes and binds to substrate polypeptides independent of DnaJ, as in the case of 32 (24). Because most o
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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
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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
1
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