DOI: 10.1073/pnas.94.2.463. Activities of human recombination protein Rad51

Activities of human recombination protein Rad51

10.1073/pnas.94.2.463

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

Abstract

Homologous pairing and strand exchange, which are catalyzed by Escherichia coli RecA protein, are central to homologous recombination. Homologs of this protein are found in eukaryotes; however, little has been reported on the recombinase activities of the mammalian homologs, including the human protein, denoted HsRad51. For the studies described here, we purified HsRad51 from E. coli . Although the activities of HsRad51 and RecA were qualitatively similar in the presence of ATP, there were also striking differences. The stoichiometry of binding to DNA and the rate of renaturation of complementary strands were similar for the two proteins, but rates of ATP hydrolysis, homologous pairing, and subsequent strand exchange promoted by HsRad51 were less than (null)/1;10 those of RecA. In addition, HsRad51 bound γ-thio-ATP and formed stable presynaptic complexes that promoted renaturation as rapidly as RecA, but the recombinant human protein catalyzed neither strand exchange nor homologous pairing of a single strand with duplex DNA in the presence of the ATP analog. By contrast, RecA promoted both of the latter reactions in control experiments. These observations suggest that among RecA-like proteins, HsRad51 may be a variant in which homologous pairing and strand exchange are more closely linked to the hydrolysis of ATP.

Bibliography

Gupta, R. C., Bazemore, L. R., Golub, E. I., & Radding, C. M. (1997). Activities of human recombination proteinâRad51. Proceedings of the National Academy of Sciences, 94(2), 463â468.

Authors 4

Ravindra C. Gupta (first)
L. Rochelle Bazemore (additional)
Efim I. Golub (additional)
Charles M. Radding (additional)

References 35 Referenced 204

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Dates

Type	When
Created	23 years ago (July 26, 2002, 10:40 a.m.)
Deposited	3 years, 4 months ago (April 13, 2022, 3:18 p.m.)
Indexed	2 weeks, 6 days ago (Aug. 5, 2025, 8:43 a.m.)
Issued	28 years, 7 months ago (Jan. 21, 1997)
Published	28 years, 7 months ago (Jan. 21, 1997)
Published Online	28 years, 7 months ago (Jan. 21, 1997)
Published Print	28 years, 7 months ago (Jan. 21, 1997)

Funders 0

None

BibTeX

@article{Gupta_1997, title={Activities of human recombination protein Rad51}, volume={94}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.94.2.463}, DOI={10.1073/pnas.94.2.463}, number={2}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Gupta, Ravindra C. and Bazemore, L. Rochelle and Golub, Efim I. and Radding, Charles M.}, year={1997}, month=jan, pages={463–468} }

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  "abstract": "<jats:p>\n            Homologous pairing and strand exchange, which are catalyzed by\n            <jats:italic>Escherichia coli</jats:italic>\n            RecA protein, are central to homologous recombination. Homologs of this protein are found in eukaryotes; however, little has been reported on the recombinase activities of the mammalian homologs, including the human protein, denoted HsRad51. For the studies described here, we purified HsRad51 from\n            <jats:italic>E. coli</jats:italic>\n            . Although the activities of HsRad51 and RecA were qualitatively similar in the presence of ATP, there were also striking differences. The stoichiometry of binding to DNA and the rate of renaturation of complementary strands were similar for the two proteins, but rates of ATP hydrolysis, homologous pairing, and subsequent strand exchange promoted by HsRad51 were less than (null)/1;10 those of RecA. In addition, HsRad51 bound \u03b3-thio-ATP and formed stable presynaptic complexes that promoted renaturation as rapidly as RecA, but the recombinant human protein catalyzed neither strand exchange nor homologous pairing of a single strand with duplex DNA in the presence of the ATP analog. By contrast, RecA promoted both of the latter reactions in control experiments. These observations suggest that among RecA-like proteins, HsRad51 may be a variant in which homologous pairing and strand exchange are more closely linked to the hydrolysis of ATP.\n          </jats:p>",
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