Inter-subunit interactions that coordinate Rad51's activities.
Inter-subunit interactions that coordinate Rad51's activities.
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DOI：
10.1093/nar/gkn973
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发表时间：
2009-02
影响因子：
14.9
通讯作者：
Rice PA
中科院分区：
文献类型：
--
作者：
Grigorescu AA;Vissers JH;Ristic D;Pigli YZ;Lynch TW;Wyman C;Rice PA
Rad51 is the central catalyst of homologous recombination in eukaryotes and is thus critical for maintaining genomic integrity. Recent crystal structures of filaments formed by Rad51 and the closely related archeal RadA and eubacterial RecA proteins place the ATPase site at the protomeric interface. To test the relevance of this feature, we mutated conserved residues at this interface and examined their effects on key activities of Rad51: ssDNA-stimulated ATP hydrolysis, DNA binding, polymerization on DNA substrates and catalysis of strand-exchange reactions. Our results show that the interface seen in the crystal structures is very important for nucleoprotein filament formation. H352 and R357 of yeast Rad51 are essential for assembling the catalytically competent form of the enzyme on DNA substrates and coordinating its activities. However, contrary to some previous suggestions, neither of these residues is critical for ATP hydrolysis.
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