Structure and Function of the Small MutS-Related Domain.
Structure and Function of the Small MutS-Related Domain.
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DOI：
10.4061/2011/691735
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发表时间：
2011
期刊：
影响因子：
--
通讯作者：
Kuramitsu S
中科院分区：
文献类型：
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作者：
Fukui K;Kuramitsu S
MutS家族蛋白广泛存在于从细菌到人类的几乎所有生物中，并在DNA错配修复和重组事件等各种DNA交易中发挥核心作用。小的MutS相关（Smr）结构域最初发现于抗重组蛋白MutS2的c端结构域，MutS2是MutS家族的一员。MutS2被认为通过核内溶解早期中间体来抑制同源重组。MutS2的内切酶活性来源于Smr结构域。有趣的是，Smr结构域的同源序列在除MutS2以外的多种蛋白质中都很丰富，可分为3个亚家族。最近报道了所有3个Smr亚家族的三级结构和内切酶活性。本文综述了含Smr结构域的生物化学特征和结构，以及含Smr蛋白的细胞功能。
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.