Rashid N, Morikawa M, Imanaka T
Department of Biotechnology, Faculty of Engineering, Osaka University, Japan.
Mol Gen Genet. 1996 Dec 13;253(3):397-400. doi: 10.1007/s004380050337.
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.
编码来自嗜热古菌火球菌属（Pyrococcus sp.）KOD1株（Pk）的RecA/RAD51同源物的基因被克隆、测序并在大肠杆菌中表达。将推导的210个氨基酸序列与来自细菌（RecA）、真核生物（RAD51、DMC1）和古菌（RadA）的同源物进行比较。来自Pk的完整蛋白质（Pk-REC）基本上对应于其对应物的必需中央结构域，并且在N端和C端缺少两个较小的RecA亚结构域。序列比较表明，Pk-REC代表具有更高酶活性的RecA、RAD51、DMC1和RadA的共同原型。重组Pk-REC具有完全活性，并弥补了大肠杆菌recA突变株对紫外线的敏感性。
