A RecA/RAD51 homologue from a hyperthermophilic archaeon retains the major RecA domain only.
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.
Rashid
N
N
Department of Biotechnology, Faculty of Engineering, Osaka University, Japan.
Morikawa
M
M
Imanaka
T
T
D000595:Amino Acid Sequence; D001105:Archaea / Q000737:chemistry / Q000235:genetics*; D019843:Archaeal Proteins; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D001483:Base Sequence; D003001:Cloning, Molecular; D004269:DNA, Bacterial; D004268:DNA-Binding Proteins / Q000737:chemistry*; D004926:Escherichia coli; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D051135:Rad51 Recombinase; D011938:Rec A Recombinases / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid
D019843:Archaeal Proteins; D001426:Bacterial Proteins; D004269:DNA, Bacterial; D004268:DNA-Binding Proteins; C103757:Pk-REC protein, Pyrococcus sp.; D051135:Rad51 Recombinase; D011938:Rec A Recombinases