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, I54A 32, a very stable mutant, is more susceptible to ClpYQ and FtsH proteases than wild-type 32, indicating that the stability of 32 does not always reflect its susceptibility to proteases. Co-precipitation and gel filtration analyses show that purified 32 mutants exhibit a reduced affinity for DnaJ, leading to a marked decrease in forming a complex with DnaK in the presence of DnaJ and ATP. Ot

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