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2
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A novel single-stranded DNA-specific 3'-5' exonuclease, Thermus thermophilus exonuclease I, is involved in several DNA repair pathways.一种新型的单链DNA特异性3'-5'核酸外切酶,嗜热栖热菌核酸外切酶I,参与多种DNA修复途径。
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Nuclease activity of the MutS homologue MutS2 from Thermus thermophilus is confined to the Smr domain.嗜热栖热菌的MutS同源物MutS2的核酸酶活性局限于Smr结构域。
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6
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7
Affinity of mismatch-binding protein MutS for heteroduplexes containing different mismatches.错配结合蛋白MutS对含有不同错配的异源双链体的亲和力。
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8
Genetic analysis of an incomplete mutS gene from Pseudomonas putida.恶臭假单胞菌中一个不完整mutS基因的遗传分析。
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9
Heteroduplex DNA and ATP induced conformational changes of a MutS mismatch repair protein from Thermus aquaticus.异源双链DNA和ATP诱导嗜热水生栖热菌MutS错配修复蛋白的构象变化。
Biochem J. 2000 May 1;347 Pt 3(Pt 3):881-6.

嗜热栖热菌MutS蛋白的结构域组织与功能分析

Domain organization and functional analysis of Thermus thermophilus MutS protein.

作者信息

Tachiki H, Kato R, Masui R, Hasegawa K, Itakura H, Fukuyama K, Kuramitsu S

机构信息

Department of Biology, Graduate School of Science, Osaka University, 1-1 Machikaneyama-cho, Toyonaka, Osaka 560-0043, Japan.

出版信息

Nucleic Acids Res. 1998 Sep 15;26(18):4153-9. doi: 10.1093/nar/26.18.4153.

DOI:10.1093/nar/26.18.4153
PMID:9722634
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC147827/
Abstract

MutS protein binds to DNA and specifically recognizes mismatched or small looped out heteroduplex DNA. In order to elucidate its structure-function relationships, the domain structure of Thermus thermophilus MutS protein was studied by performing denaturation experiments and limited proteolysis. The former suggested that T. thermophilus MutS consists of at least three domains with estimated stabilities of 12.3, 22.9 and 30.7 kcal/mol and the latter revealed that it consists of four domains: A1 (N-terminus to residue 130), A2 (131-274), B (275-570) and C (571 to C-terminus). A gel retardation assay indicated that T.thermophilus MutS interacts non-specifically with double-stranded (ds), but not single-stranded DNA. Among the proteolytic fragments, the B domain bound to dsDNA. On the basis of these results we have proposed the domain organization of T. thermophilus MutS and putative roles of these domains.

摘要

MutS蛋白与DNA结合,并特异性识别错配或小的环状异源双链DNA。为了阐明其结构-功能关系,通过进行变性实验和有限蛋白酶解研究了嗜热栖热菌MutS蛋白的结构域结构。前者表明嗜热栖热菌MutS至少由三个结构域组成,估计稳定性分别为12.3、22.9和30.7千卡/摩尔,后者表明它由四个结构域组成:A1(N端至第130位残基)、A2(131-274)、B(275-570)和C(571至C端)。凝胶阻滞试验表明,嗜热栖热菌MutS与双链(ds)而非单链DNA非特异性相互作用。在蛋白水解片段中,B结构域与dsDNA结合。基于这些结果,我们提出了嗜热栖热菌MutS的结构域组织以及这些结构域的假定作用。