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.
journal_name
Proc Natl Acad Sci U S Aauthors
Li Z,Golub EI,Gupta R,Radding CMdoi
10.1073/pnas.94.21.11221subject
Has Abstractpub_date
1997-10-14 00:00:00pages
11221-6issue
21eissn
0027-8424issn
1091-6490journal_volume
94pub_type
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