Characterization of a RecA/RAD51 homologue from the hyperthermophilic archaeon Pyrococcus sp. KOD1.

Abstract:

:The Pk-rec gene, encoding a RecA/RAD51 homologue from the hyperthermophilic archaeon Pyrococcussp. KOD1, was expressed in Escherichia coli. The recombinant Pk-REC was purified to homogeneity and was shown to be in a dimeric form. A striking property of the purified recombinant Pk-REC was the unusual DNase activity on both single- and double-stranded DNAs along with the ATPase activity. The reaction product of this DNase activity was mononucleotides. The optimum temperature and pH for the DNase activity were 60 degrees C and 8-8.5, respectively. In addition, the metal ion requirement for DNase activity was different from that for the ATPase activity. The protein exhibited no DNase activity in the presence of Zn2+ion, which was one of the most preferable divalent cations for ATPase activity. Another unique characteristic of the recombinant protein was that the reaction product of ATPase activity was AMP instead of ADP.Pk-REC may represent a common prototype of the RecA family proteins with high RecA-like activity.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Rashid N,Morikawa M,Nagahisa K,Kanaya S,Imanaka T

doi

10.1093/nar/25.4.719

subject

Has Abstract

pub_date

1997-02-15 00:00:00

pages

719-26

issue

4

eissn

0305-1048

issn

1362-4962

pii

gka149

journal_volume

25

pub_type

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