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嗜热栖热菌HB8 MutS的错配及插入/缺失结合特性分析

Analysis of the mismatch and insertion/deletion binding properties of Thermus thermophilus, HB8, MutS.

作者信息

Whitehouse A, Deeble J, Parmar R, Taylor G R, Markham A F, Meredith D M

机构信息

Molecular Medicine Unit, University of Leeds, St. James's University Hospital, United Kingdom.

出版信息

Biochem Biophys Res Commun. 1997 Apr 28;233(3):834-7. doi: 10.1006/bbrc.1997.6551.

DOI:10.1006/bbrc.1997.6551
PMID:9168943
Abstract

The methyl-directed long patch repair pathway in Escherichia coli is involved in increasing the fidelity of replication specific repair of DNA polymerase incorporation errors. This pathway is mediated by three gene products, MutS, MutL, and MutH, which are conserved in higher eukaryotes. Mutations in human homologues of these proteins have been shown to be implicated in hereditary non-polyposis colorectal cancer (HNPCC). A MutS homologue has recently been identified in the extremely thermophilic bacterium, Thermus thermophilus. Here we describe analysis of the binding properties of this protein, which has indicated it can identify all specific base mismatches as well as one, two and three base pair insertion/deletion mutations. We therefore believe this protein may be generally useful for applications involving mismatch detection.

摘要

大肠杆菌中的甲基导向长片段修复途径参与提高DNA聚合酶掺入错误的复制特异性修复的保真度。该途径由三种基因产物介导,即MutS、MutL和MutH,它们在高等真核生物中是保守的。这些蛋白质的人类同源物中的突变已被证明与遗传性非息肉病性结直肠癌(HNPCC)有关。最近在嗜热栖热菌这种极端嗜热细菌中鉴定出了一种MutS同源物。在此,我们描述了对该蛋白质结合特性的分析,结果表明它可以识别所有特定的碱基错配以及一、二和三个碱基对的插入/缺失突变。因此,我们认为这种蛋白质可能普遍适用于涉及错配检测的应用。

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1
Analysis of the mismatch and insertion/deletion binding properties of Thermus thermophilus, HB8, MutS.嗜热栖热菌HB8 MutS的错配及插入/缺失结合特性分析
Biochem Biophys Res Commun. 1997 Apr 28;233(3):834-7. doi: 10.1006/bbrc.1997.6551.
2
Mismatch DNA recognition protein from an extremely thermophilic bacterium, Thermus thermophilus HB8.来自嗜热栖热菌HB8的错配DNA识别蛋白。
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Directly fishing out subtle mutations in genomic DNA with histidine-tagged Thermus thermophilus MutS.使用组氨酸标签的嗜热栖热菌MutS直接筛选基因组DNA中的细微突变。
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DNA mismatch correction in Haemophilus influenzae: characterization of MutL, MutH and their interaction.流感嗜血杆菌中的DNA错配修复:MutL、MutH的特性及其相互作用
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A carboxy terminal domain of the hMSH-2 gene product is sufficient for binding specific mismatched oligonucleotides.人错配修复蛋白2(hMSH-2)基因产物的羧基末端结构域足以结合特定的错配寡核苷酸。
Biochem Biophys Res Commun. 1996 Aug 5;225(1):289-95. doi: 10.1006/bbrc.1996.1168.
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Direct observation of three conformations of MutS protein regulated by adenine nucleotides.直接观察由腺嘌呤核苷酸调节的MutS蛋白的三种构象。
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Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA.错配修复蛋白MutS的晶体结构及其与底物DNA的复合物
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The crystal structure of DNA mismatch repair protein MutS binding to a G x T mismatch.DNA错配修复蛋白MutS与G×T错配结合的晶体结构。
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Guarding against mutation.防范突变。
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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.

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