Abstract
Homologous DNA recombination promotes genetic diversity and the maintenance of genome integrity, yet no enzymes with specificity for the Holliday junction (HJ)—a key DNA recombination intermediate—have been purified and characterized from metazoa or their viruses. Here we identify critical structural elements of RuvC, a bacterial HJ resolvase, in uncharacterized open reading frames from poxviruses and an iridovirus. The putative vaccinia virus resolvase was expressed as a recombinant protein, affinity purified, and shown to specifically bind and cleave a synthetic HJ to yield nicked duplex molecules. Mutation of either of two conserved acidic amino acids abrogated the catalytic activity of the A22R protein without affecting HJ binding. The presence of bacterial-type enzymes in metazoan viruses raises evolutionary questions.
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Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 26, 2002, 10:32 a.m.) |
Deposited | 3 years, 4 months ago (April 12, 2022, 11:37 p.m.) |
Indexed | 1 month, 3 weeks ago (July 11, 2025, 6:49 a.m.) |
Issued | 25 years, 1 month ago (July 11, 2000) |
Published | 25 years, 1 month ago (July 11, 2000) |
Published Online | 25 years, 1 month ago (July 11, 2000) |
Published Print | 25 years, 1 month ago (Aug. 1, 2000) |
@article{Garcia_2000, title={Bacterial-type DNA Holliday junction resolvases in eukaryotic viruses}, volume={97}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.150238697}, DOI={10.1073/pnas.150238697}, number={16}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Garcia, Alonzo D. and Aravind, L. and Koonin, Eugene V. and Moss, Bernard}, year={2000}, month=jul, pages={8926–8931} }