来自嗜盐古菌红皮盐杆菌的一种亲环蛋白型肽基脯氨酰顺反异构酶的基因。

Gene for a cyclophilin-type peptidyl-prolyl cis-trans isomerase from a halophilic archaeum, Halobacterium cutirubrum.

作者信息

Iida T, Furutani M, Iwabuchi T, Maruyama T

机构信息

Marine Biotechnology Institute, Kamaishi Laboratories, Iwate, Japan.

出版信息

Gene. 1997 Dec 19;204(1-2):139-44. doi: 10.1016/s0378-1119(97)00534-9.

DOI:10.1016/s0378-1119(97)00534-9

PMID:9434176

Abstract

A gene encoding a cyclophilin (CyP)-type peptidyl prolyl cis-trans isomerase (PPIase) was cloned from a halophilic archaeum, Halobacterium cutirubrum DSM 669, and sequenced. Although amino-acid residues common to CyPs were conserved, an insertion that showed no homology to other CyPs was found in its N-terminal region. Sequence analysis revealed that the amino-acid sequence of this CyP was 40-45% identical to those of eukaryotes and Bacillus subtilis with high cyclosporin A sensitivity, but 27% identical to those of cyclosporin A-insensitive PPIases of Escherichia coli. The gene was also expressed in E. coli. The activity of purified recombinant CyP-type PPIase was stimulated by the addition of KCl, and was suppressed by cyclosporin A.

摘要

从嗜盐古菌红皮盐杆菌DSM 669中克隆并测序了一个编码亲环蛋白（CyP）型肽基脯氨酰顺反异构酶（PPIase）的基因。虽然CyP共有的氨基酸残基是保守的，但在其N端区域发现了一个与其他CyP无同源性的插入序列。序列分析表明，该CyP的氨基酸序列与对环孢菌素A敏感的真核生物和枯草芽孢杆菌的氨基酸序列有40%-45%的同一性，但与大肠杆菌对环孢菌素A不敏感的PPIase的氨基酸序列有27%的同一性。该基因也在大肠杆菌中表达。纯化的重组CyP型PPIase的活性在添加KCl时受到刺激，而在添加环孢菌素A时受到抑制。