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Science 26 March 1993: Vol. 259. no. 5103, pp. 1896 - 1899 DOI: 10.1126/science.8456314
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Articles
Science, Vol 259, Issue 5103, 1896-1899
Copyright © 1993 by American Association for the Advancement of Science
Similarity of the yeast RAD51 filament to the bacterial RecA filament
T Ogawa,
X Yu,
A Shinohara,
and
EH Egelman
Department of Biology, Osaka University, Japan.
The RAD51 protein functions in the processes of DNA repair and in mitotic and meiotic genetic recombination in the yeast Saccharomyces cerevisiae. The protein has adenosine triphosphate-dependent DNA binding activities similar to those of the Escherichia coli RecA protein, and the two proteins have 30 percent sequence homology. RAD51 polymerized on double-stranded DNA to form a helical filament nearly identical in low-resolution, three-dimensional structure to that formed by RecA. Like RecA, RAD51 also appears to force DNA into a conformation of approximately a 5.1-angstrom rise per base pair and 18.6 base pairs per turn. As in other protein families, its structural conservation appears to be stronger than its sequence conservation. Both the structure of the protein polymer formed by RecA and the DNA conformation induced by RecA appear to be general properties of a class of recombination proteins found in prokaryotes as well as eukaryotes.
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- Human Rad51 Protein Can Form Homologous Joints in the Absence of Net Strand Exchange.
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- Sequestration of Mammalian Rad51-Recombination Protein into Micronuclei.
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- The Human Rad54 Recombinational DNA Repair Protein Is a Double-stranded DNA-dependent ATPase.
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- Base pair switching by interconversion of sugar puckers in DNA extended by proteins of RecA-family: A model for homology search in homologous genetic recombination.
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PNAS
95, 11071-11076
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- Polarity of DNA strand exchange promoted by recombination proteins of the RecA family.
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PNAS
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