Tao Y, Li X, Liu Y, Ruan J, Qi S, Niu L, Teng M

The yeast Shu complex, consisting of the proteins Shu1, Shu2, Psy3 and Csm2, maintains genomic stability by coupling post-replication repair to homologous recombination. However, a lack of biochemical and structural information on the Shu proteins precludes revealing their precise roles within the pathway. Here we report the 1.9 A crystal ...

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structure of the Psy3-Csm2 complex. The crystal structure shows that Psy3 forms a heterodimer with Csm2 mainly through a hydrophobic core. Unexpectedly, Psy3 and Csm2 share a similar architecture which closely resembles the ATPase core domain of Rad51. The L2 loop present in Psy3 and Csm2 is similar to that of Rad51, and confers the DNA-binding activity of the Shu complex. As with Rad51, the Shu complex appears to form a nucleoprotein filament by binding non-specifically to DNA. Structure-based mutagenesis studies have demonstrated that the DNA-binding activity of the Shu complex is essential for repair of the methyl methanesulfonate-induced DNA damage. Our findings provide good foundations for the understanding of the Srs2 regulation by the Shu complex.

Date: Mar. 30, 2012

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