Rommelaere H, Van Troys M, Gao Y, Melki R, Cowan N J, Vandekerckhove J, Ampe C
Laboratory of Physiological Chemistry, University Ghent, Belgium.
Proc Natl Acad Sci U S A. 1993 Dec 15;90(24):11975-9. doi: 10.1073/pnas.90.24.11975.
We have characterized the cytosolic chaperonin from both rabbit reticulocyte lysate and bovine testis. The heteromeric complex contains eight subunits. Partial amino acid sequence data reveal that one of these is t-complex polypeptide 1 (TCP-1), while the other seven are TCP-1-related polypeptides, implicating the existence of a multigene family of TCP-1 homologues. We provide evidence that TCP-1 ring complex from bovine testis can facilitate the folding of both actin and tubulin, although, as in the case of chaperonin from reticulocyte lysate, two cofactors are required for the generation of properly folded tubulin. An additional molecule of TCP-1 may associate with the chaperonin depending on the purification procedure used. We propose that a highly conserved region in these polypeptides and in other chaperonins of the cpn60 chaperone family participates in ATP binding.
我们已经对来自兔网织红细胞裂解物和牛睾丸的胞质伴侣蛋白进行了表征。该异源复合物包含八个亚基。部分氨基酸序列数据显示其中一个是t-复合物多肽1（TCP-1），而其他七个是与TCP-1相关的多肽，这意味着存在TCP-1同源物的多基因家族。我们提供的证据表明，来自牛睾丸的TCP-1环复合物可以促进肌动蛋白和微管蛋白的折叠，尽管与网织红细胞裂解物中的伴侣蛋白一样，生成正确折叠的微管蛋白需要两种辅助因子。根据所使用的纯化程序，额外的TCP-1分子可能与伴侣蛋白结合。我们提出，这些多肽以及cpn60伴侣蛋白家族的其他伴侣蛋白中的一个高度保守区域参与ATP结合。
