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Structure and Function of the Small MutS-Related Domain
MutS family proteins are widely distributed in almost all organisms from bacteria to human and play central roles in various DNA transactions such as DNA mismatch repair and recombinational events. The small MutS-related (Smr) domain was originally found in the C-terminal domain of an antirecombinat...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
SAGE-Hindawi Access to Research
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3200294/ https://www.ncbi.nlm.nih.gov/pubmed/22091410 http://dx.doi.org/10.4061/2011/691735 |
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author | Fukui, Kenji Kuramitsu, Seiki |
author_facet | Fukui, Kenji Kuramitsu, Seiki |
author_sort | Fukui, Kenji |
collection | PubMed |
description | MutS family proteins are widely distributed in almost all organisms from bacteria to human and play central roles in various DNA transactions such as DNA mismatch repair and recombinational events. The small MutS-related (Smr) domain was originally found in the C-terminal domain of an antirecombination protein, MutS2, a member of the MutS family. MutS2 is thought to suppress homologous recombination by endonucleolytic resolution of early intermediates in the process. The endonuclease activity of MutS2 is derived from the Smr domain. Interestingly, sequences homologous to the Smr domain are abundant in a variety of proteins other than MutS2 and can be classified into 3 subfamilies. Recently, the tertiary structures and endonuclease activities of all 3 Smr subfamilies were reported. In this paper, we review the biochemical characteristics and structures of the Smr domains as well as cellular functions of the Smr-containing proteins. |
format | Online Article Text |
id | pubmed-3200294 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | SAGE-Hindawi Access to Research |
record_format | MEDLINE/PubMed |
spelling | pubmed-32002942011-11-16 Structure and Function of the Small MutS-Related Domain Fukui, Kenji Kuramitsu, Seiki Mol Biol Int Review Article MutS family proteins are widely distributed in almost all organisms from bacteria to human and play central roles in various DNA transactions such as DNA mismatch repair and recombinational events. The small MutS-related (Smr) domain was originally found in the C-terminal domain of an antirecombination protein, MutS2, a member of the MutS family. MutS2 is thought to suppress homologous recombination by endonucleolytic resolution of early intermediates in the process. The endonuclease activity of MutS2 is derived from the Smr domain. Interestingly, sequences homologous to the Smr domain are abundant in a variety of proteins other than MutS2 and can be classified into 3 subfamilies. Recently, the tertiary structures and endonuclease activities of all 3 Smr subfamilies were reported. In this paper, we review the biochemical characteristics and structures of the Smr domains as well as cellular functions of the Smr-containing proteins. SAGE-Hindawi Access to Research 2011 2011-07-19 /pmc/articles/PMC3200294/ /pubmed/22091410 http://dx.doi.org/10.4061/2011/691735 Text en Copyright © 2011 K. Fukui and S. Kuramitsu. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Article Fukui, Kenji Kuramitsu, Seiki Structure and Function of the Small MutS-Related Domain |
title | Structure and Function of the Small MutS-Related Domain |
title_full | Structure and Function of the Small MutS-Related Domain |
title_fullStr | Structure and Function of the Small MutS-Related Domain |
title_full_unstemmed | Structure and Function of the Small MutS-Related Domain |
title_short | Structure and Function of the Small MutS-Related Domain |
title_sort | structure and function of the small muts-related domain |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3200294/ https://www.ncbi.nlm.nih.gov/pubmed/22091410 http://dx.doi.org/10.4061/2011/691735 |
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