在GroEL（伴侣蛋白60）伴侣蛋白中鉴定出与GroES（伴侣蛋白10）相关的序列基序。

Identification of a GroES (CPN10)-related sequence motif in the GroEL (CPN60) chaperonins.

作者信息

Gupta R S

机构信息

Department of Biochemistry, McMaster University, Hamilton, ON, Canada.

出版信息

Biochem Mol Biol Int. 1994 Jun;33(3):591-5.

PMID:7951076

Abstract

Significant sequence similarity has been noted between a segment of the 60 kDa heat shock family of proteins (designated as GroEL, cpn60 or hsp60) and its functional partner, the 10-12 kDa GroES (or cpn10) family of proteins. Upon introduction of a few gaps, 31 identical and 19 conserved residues were observed in a 93 amino acid overlap between the region comprising of a.a. 314 to 431 in E. coli GroEL and the entire GroES sequence from Bacillus subtilis. The functional forms of both GroEL and GroES proteins, which function as a team in the protein folding process, are toroidal rings exhibiting a highly unusual seven-fold rotational axis of symmetry. It is suggested that the information for assuming this structural form is contained within the shared sequence region between these proteins.

摘要

已注意到60 kDa热休克蛋白家族（称为GroEL、cpn60或hsp60）的一段序列与其功能伙伴10 - 12 kDa GroES（或cpn10）蛋白家族之间存在显著的序列相似性。引入一些空位后，在大肠杆菌GroEL中由第314至431位氨基酸组成的区域与枯草芽孢杆菌的整个GroES序列的93个氨基酸重叠区中，观察到31个相同残基和19个保守残基。在蛋白质折叠过程中协同发挥作用的GroEL和GroES蛋白的功能形式均为环形结构，呈现出极为罕见的七重旋转对称轴。有人提出，形成这种结构形式的信息包含在这些蛋白质之间的共享序列区域内。