Mammalian HSP40/DnaJ Chaperone Proteins in Cytosol
作者： Kazutoyo Terada , Masataka Mori
DOI: 10.1007/978-0-387-39717-7_11
关键词:
摘要: The HSP70-based molecular chaperone system in cytosol mediates various biological processes such as folding of newly synthesized proteins, refolding misfolded translocation proteins into organelles, assembly and their degradation (Gething Sambrook, 1992; Frydman, 2001; Young et al., 2004; Mayer Bukau, 2005). HSP70 catalyze these with the aid HSP40/DnaJ co-chaperones (Fig. 1A). initially recognize substrate polypeptides, transfer them to substrate-binding domain proteins. During or just after polypeptide HSP70, J-domain accelerates hydrolysis bound ATP nucleotide-binding HSP70. leads a conformational change bind tightly. After binding interact HSP70-polypeptide binary complex. Many mammals contain tetratricopeptide repeat (TPR) domain(s), this recognizes EEVD sequence at carboxyl-terminal cytosolic eu-karyotes. combination three components is important determine proper destination polypeptide.
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