SIMILARITY OF THE YEAST RAD51 FILAMENT TO THE BACTERIAL RECA FILAMENT

被引:575
作者
OGAWA, T
YU, X
SHINOHARA, A
EGELMAN, EH
机构
[1] UNIV MINNESOTA, SCH MED, DEPT CELL BIOL & NEUROANAT, MINNEAPOLIS, MN 55455 USA
[2] OSAKA UNIV, DEPT BIOL, TOYONAKA, OSAKA 560, JAPAN
关键词
D O I
10.1126/science.8456314
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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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页码:1896 / 1899
页数:4
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