A RecA/RAD51 homologue from a hyperthermophilic archaeon retains the major RecA domain only

被引：27

作者：

Rashid, N ^{[1
]}

Morikawa, M ^{[1
]}

Imanaka, T ^{[1
]}

机构：

[1] OSAKA UNIV,FAC ENGN,DEPT BIOTECHNOL,SUITA,OSAKA 565,JAPAN

来源：

MOLECULAR & GENERAL GENETICS | 1996年 / 253卷 / 03期

关键词：

Pyrococcus sp KOD1; RecA homologue; major domain; recombination; complementation;

D O I：

10.1007/s004380050337

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A gene encoding a RecA/RAD51 homologue from a hyperthermophilic archaeon, Pyrococcus sp. KOD1 (Pk), was cloned, sequenced and expressed in Escherichia coli. The deduced 210-amino acid sequence was compared to homologues from bacteria (RecA), eukaryotes (RAD51, DMC1) and archaea (RadA). The entire protein from Pk (Pk-REC) basically corresponds to the essential central domain of its counterparts and lacks the two smaller RecA subdomains at the N- and C-termini. The sequence comparison suggests that Pk-REC represents a common prototype of RecA, RAD51, DMC1 and RadA, with higher enzymatic activity. Recombinant Pk-REC was fully active and complemented the ultraviolet light sensitivity of an E. coli recA mutant strain.

引用

页码：397 / 400

页数：4

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