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J. Biol. Chem., Vol. 283, Issue 19, 99915, May 9, 2008
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Clamping Down on Mismatch Repair{diamondsuit}

The trimeric DNA clamp PCNA (proliferating cell nuclear antigen) helps coordinate various components of DNA replication, repair, and recombination. Among these is its interaction with the mismatch repair protein MutS{alpha}, and in this Paper of the Week, Ravi Iyer and colleagues provide elegant studies that reveal the conformation and properties of the human PCNA·MutS{alpha} complex. The two proteins associate in a 1:1 ratio in the presence or absence of duplex DNA, and x-ray scattering studies indicate they bind in an end-to-end fashion without an extended tether, as is proposed for the yeast PCNA interaction. Likewise, although previous work in yeast has suggested that PCNA enhances the affinity of MutS{alpha} for mismatches, this is not the case for human PCNA; the PCNA·MutS{alpha} complex does not influence, nor is it influenced by, mismatch binding. Interestingly, MutS{alpha} variants that cannot bind PCNA displayed only a limited defect in the rate of 5'-directed mismatch repair (3'-directed repair was unaffected), suggesting that MutS{alpha} binding is not the essential role of PCNA in mismatch repair.Go


Figure 1
Low resolution model of the end-to-end human MutS{alpha}·PCNA complex with crystal structures of MutS{alpha}{Delta}341 and PCNA.

FOOTNOTES

{diamondsuit} See referenced article, J. Biol. Chem. 2008, 283, 13310-13319 Back



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This Article
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