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DNA repair

Recognition is crystal clear

Nature Reviews Molecular Cell Biology volume 1, pages 84–85 (2000)Cite this article

DNA polymerases are not infallible — they make mistakes while replicating DNA. Sometimes these errors are deliberate. But often they are not, and that's when mismatch repair kicks in to protect against mutation. This system identifies DNA bases that have been incorrectly paired up, and allows the correct base to be reinserted. But how does it recognize the mismatches? Two groups, reporting in the 12 October issue of Nature, have studied the bacterial mismatch-repair protein MutS to address this question.

In the first paper, Obmolova et al. present the crystal structures of a Thermus aquaticus MutS homodimer, both alone and as a complex with DNA containing a single unpaired thymidine. The authors show that the DNA adopts an unusual kinked shape owing to interactions with two domains from each MutS monomer (domains I and IV; see diagram). However, these interactions are asymmetric, with domain I from monomer A in the diagram donating the phenylalanine residue (yellow ring) that interacts specifically with the unpaired base.

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References

ORIGINAL RESEARCH PAPERS

  1. Obmolova, G. et al. Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA. Nature 407, 703–710 ( 2000) [ Contents page]

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  2. Lamers, M. H. et al. The crystal structure of DNA mismatch repair protein MutS binding to a G●T mismatch. Nature 407, 711–717 (2000) [ Contents page]

    Article  CAS  Google Scholar 

FURTHER READING

  1. Kolodner, R. D. Guarding against mutation. Nature 407, 687–689 (2000) [ Contents page]

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Authors
  1. Alison Mitchell
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Mitchell, A. Recognition is crystal clear. Nat Rev Mol Cell Biol 1, 84–85 (2000). https://doi.org/10.1038/35040003

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  • DOI: https://doi.org/10.1038/35040003

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