嗜酸嗜热古菌硫磺矿硫化叶菌菌株7中II型伴侣蛋白的纯化及分子克隆

Purification and molecular cloning of the group II chaperonin from the acidothermophilic archaeon, Sulfolobus sp. strain 7.

作者信息

Nakamura N, Taguchi H, Ishii N, Yoshida M, Suzuki M, Endo I, Miura K, Yohda M

机构信息

Research Laboratory of Resources Utilization, Tokyo Institute of Technology, Yokohama, Japan.

出版信息

Biochem Biophys Res Commun. 1997 Jul 30;236(3):727-32. doi: 10.1006/bbrc.1997.6916.

DOI:10.1006/bbrc.1997.6916

PMID:9245723

Abstract

To elucidate the structure and functional mechanism of the group II chaperonin, molecular cloning of the gene for and purification of the group II chaperonin from the thermoacidophilic archaeon Sulfolobus sp. strain 7 were performed. The purified Sulfolobus chaperonin exhibited weak ATPase activity and arrested the spontaneous refolding of the thermophilic lactate dehydrogenase. However, the refolding could not be resumed by addition of ATP. The chaperonin consists of two kinds of subunits, alpha and beta, the deduced amino acid sequences of which were highly homologous to those of TF56 and TF55 from Sulfolobus shibatae, respectively.

摘要

为阐明Ⅱ型伴侣蛋白的结构和功能机制，我们进行了来自嗜热嗜酸古菌硫磺硫杆菌菌株7的Ⅱ型伴侣蛋白基因的分子克隆及该蛋白的纯化。纯化后的硫磺硫杆菌伴侣蛋白表现出较弱的ATP酶活性，并能抑制嗜热乳酸脱氢酶的自发重折叠。然而，添加ATP后重折叠过程无法恢复。该伴侣蛋白由α和β两种亚基组成，其推导的氨基酸序列分别与来自柴田硫磺硫杆菌的TF56和TF55高度同源。