Recombination activities of HsDmc1 protein, the meiotic human homolog of RecA protein.

Abstract:

:Meiosis-specific homologs of RecA protein have been identified in Saccharomyces cerevisiae and higher eukaryotes including mammals, but their enzymatic activities have not been described. We have purified the human protein HsDmc1 produced in Escherichia coli from a cloned copy of the cDNA. The recombinant enzyme had DNA-dependent ATPase activity with an estimated kcat of 1.5 min-1. DNase protection experiments with oligonucleotides as substrates indicated that HsDmc1 protein binds preferentially to single-stranded DNA with a stoichiometry of approximately one molecule of protein per three nucleotide residues. HsDmc1 protein catalyzed the formation of D-loops in superhelical DNA, as well as strand exchange between single-stranded and double-stranded oligonucleotides. The requirements for strand exchange catalyzed by HsDmc1 were similar to those of RecA protein, but exchange caused by HsDmc1 was not supported by ATPgammaS.

authors

Li Z,Golub EI,Gupta R,Radding CM

doi

10.1073/pnas.94.21.11221

subject

Has Abstract

pub_date

1997-10-14 00:00:00

pages

11221-6

issue

21

eissn

0027-8424

issn

1091-6490

journal_volume

94

pub_type

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