Trends Cell Biol. 1997 Mar;7(3):129-33. doi: 10.1016/S0962-8924(96)10056-8.
The characterization of molecular chaperones is of central importance for an understanding of cellular protein-folding reactions. Numerous biochemical and genetic studies have now been complemented by the high-resolution structures of Hsp70 and GroEL, representatives of the two major classes of chaperone proteins, and the availability of a complete eukaryotic genome, revealing the presence of 14 distinct genes for Hsp70s in the yeast Saccharomyces cerevisiae. Here, the authors focus on recent progress in understanding the interactions of Hsp70s with their substrates and the enzymology of their regulation.
分子伴侣的特征对于理解细胞内蛋白质折叠反应至关重要。现在,大量的生化和遗传学研究已经被 HSP70 和 GroEL 的高分辨率结构所补充,这两种主要的伴侣蛋白代表了,以及完整的真核基因组的可用性,揭示了酵母酿酒酵母中存在 14 种不同的 Hsp70 基因。在这里,作者专注于理解 Hsp70 与其底物相互作用以及其调控酶学的最新进展。