Evstigneeva Z G, Solov'eva N A, Sidel'nikova L I
Bach Institute of Biochemistry, Russian Academy of Sciences, Leninskii pr. 33, Moscow, 117071 Russia.
Prikl Biokhim Mikrobiol. 2001 Jan-Feb;37(1):5-18.
Folding and assembling of newly synthesized proteins is directed and effected by a group of relatively recently discovered proteins called molecular chaperones. These proteins not only control the assembling of native structures; they also remodel protein molecules that have wrong conformations. All molecular chaperones perform the same function, but structurally they are divided into groups of chaperones and chaperonins. These proteins are highly conserved in evolution and display an ATPase activity. Certain known chaperones and chaperonins are shown in the table, and their structures and mechanisms of action are described.
新合成蛋白质的折叠和组装由一组相对较新发现的称为分子伴侣的蛋白质指导并实现。这些蛋白质不仅控制天然结构的组装;它们还重塑具有错误构象的蛋白质分子。所有分子伴侣都执行相同的功能,但在结构上它们分为伴侣蛋白和伴侣素组。这些蛋白质在进化过程中高度保守,并具有ATP酶活性。表中列出了某些已知的伴侣蛋白和伴侣素,并描述了它们的结构和作用机制。