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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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Ytoplasm. It is known to degrade some cytoplasmic proteins as well as membrane proteins (7). Although FtsH is essential for growth, a ftsH strain can be isolated if the cell simultaneously contains an unusually high activity of R-3-hydroxyacyl-ACP dehydrase (encoded by the fabZ gene) (8). The major function of FtsH is the maintenance of the proper lipopolysaccharide/ phospholipids ratio by the deg
1
Ytoplasm. It is known to degrade some cytoplasmic proteins as well as membrane proteins (7). Although FtsH is essential for growth, a ftsH strain can be isolated if the cell simultaneously contains an unusually high activity of R-3-hydroxyacyl-ACP dehydrase (encoded by the fabZ gene) (8). The major function of FtsH is the maintenance of the proper lipopolysaccharide/ phospholipids ratio by the deg
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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
, 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
1
, 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
1
, 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