家族成员：非典型热休克蛋白70伴侣蛋白是热休克蛋白70活性的保守调节因子。
All in the family: atypical Hsp70 chaperones are conserved modulators of Hsp70 activity.
作者信息
Shaner Lance, Morano Kevin A
机构信息
Department of Microbiology and Molecular Genetics, University of Texas Medical School, 6431 Fannin St., Houston, TX 77030, USA.
出版信息
Cell Stress Chaperones. 2007 Spring;12(1):1-8. doi: 10.1379/csc-245r.1.
Abstract
Divergent relatives of the Hsp70 protein chaperone such as the Hsp110 and Grp170 families have been recognized for some time, yet their biochemical roles remained elusive. Recent work has revealed that these "atypical" Hsp70s exist in stable complexes with classic Hsp70s where they exert a powerful nucleotide-exchange activity that synergizes with Hsp40/DnaJ-type cochaperones to dramatically accelerate Hsp70 nucleotide cycling. This represents a novel evolutionary transition from an independent protein-folding chaperone to what appears to be a dedicated cochaperone. Contributions of the atypical Hsp70s to established cellular roles for Hsp70 now must be deciphered.
摘要
热休克蛋白70（Hsp70）蛋白伴侣的不同亲属，如Hsp110和Grp170家族，已经被认识了一段时间，但其生化作用仍然难以捉摸。最近的研究表明，这些“非典型”Hsp70与经典Hsp70形成稳定复合物，在其中发挥强大的核苷酸交换活性，与Hsp40/DnaJ型共伴侣协同作用，显著加速Hsp70核苷酸循环。这代表了从独立的蛋白质折叠伴侣到似乎是专用共伴侣的一种新型进化转变。现在必须解读非典型Hsp70对Hsp70既定细胞作用的贡献。
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