Nucleic Acids Research Advance Access originally published online on January 10, 2007
Nucleic Acids Research 2007 35(3):850-860; doi:10.1093/nar/gkl735
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Nucleic Acids Research, 2007, Vol. 35, No. 3 850-860
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Molecular Biology |
Nuclease activity of the MutS homologue MutS2 from Thermus thermophilus is confined to the Smr domain
1 Department of Biological Sciences, Graduate School of Science, Osaka University Toyonaka, Osaka 560-0043, Japan 2 RIKEN SPring-8 Center, Harima Institute 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan
*To whom correspondence should be addressed at Department of Biology, Graduate School of Science, Osaka University, 1-1 Machikaneyamacho, Toyonaka, Osaka 560-0043, Japan. Tel: +81 06 6850 5433; Fax: +81 06 6850 5442; Email: rmasui{at}bio.sci.osaka-u.ac.jp
Received July 8, 2006. Revised September 13, 2006. Accepted September 14, 2006.
MutS homologues are highly conserved enzymes engaged in DNA mismatch repair (MMR), meiotic recombination and other DNA modifications. Genome sequencing projects have revealed that bacteria and plants possess a MutS homologue, MutS2. MutS2 lacks the mismatch-recognition domain of MutS, but contains an extra C-terminal region called the small MutS-related (Smr) domain. Sequences homologous to the Smr domain are annotated as ‘proteins of unknown function’ in various organisms ranging from bacteria to human. Although recent in vivo studies indicate that MutS2 plays an important role in recombinational events, there had been only limited characterization of the biochemical function of MutS2 and the Smr domain. We previously established that Thermus thermophilus MutS2 (ttMutS2) possesses endonuclease activity. In this study, we report that a Smr-deleted ttMutS2 mutant retains the dimerization, ATPase and DNA-binding activities, but has no endonuclease activity. Furthermore, the Smr domain alone was stable and functional in binding and incising DNA. It is noteworthy that an endonuclease activity is associated with a MutS homologue, which is generally thought to recognize specific DNA structures.
DDBJ/EMBL/GenBank accession no. AB107662 [GenBank]
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