hMYH的功能表达，它是大肠杆菌MutY蛋白的人类同源物。
Functional expression of hMYH, a human homolog of the Escherichia coli MutY protein.
作者信息
Slupska M M, Luther W M, Chiang J H, Yang H, Miller J H
机构信息
Department of Microbiology and Molecular Genetics and the Molecular Biology Institute, University of California, Los Angeles, California 90095, USA.
出版信息
J Bacteriol. 1999 Oct;181(19):6210-3. doi: 10.1128/JB.181.19.6210-6213.1999.
Abstract
We have previously described the hMYH cDNA and genomic clones (M. M. Slupska et al., J. Bacteriol. 178:3885-3892, 1996). Here, we report that the enzyme expressed from an hMYH cDNA clone in Escherichia coli complements the mutator phenotype in a mutY mutant and can remove A from an A. 8-hydroxydeoxyguanine mismatch and to a lesser extent can remove A from an A. G mismatch in vitro.
摘要
我们之前已经描述了hMYH cDNA和基因组克隆（M.M.斯卢普斯卡等人，《细菌学杂志》178:3885 - 3892，1996年）。在此，我们报告从hMYH cDNA克隆在大肠杆菌中表达的酶可弥补mutY突变体中的诱变表型，并且在体外能够从A·8 - 羟基脱氧鸟嘌呤错配中去除A，在较小程度上也能从A·G错配中去除A。
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MutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamily.MutY催化核心、突变体及结合腺嘌呤的结构决定了DNA修复酶超家族的特异性。
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Evidence that MutY is a monofunctional glycosylase capable of forming a covalent Schiff base intermediate with substrate DNA.MutY是一种单功能糖基化酶，能够与底物DNA形成共价席夫碱中间体的证据。
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Escherichia coli MutY protein has a guanine-DNA glycosylase that acts on 7,8-dihydro-8-oxoguanine:guanine mispair to prevent spontaneous G:C-->C:G transversions.大肠杆菌MutY蛋白具有一种鸟嘌呤-DNA糖基化酶，该酶作用于7,8-二氢-8-氧代鸟嘌呤与鸟嘌呤的错配，以防止自发的G:C→C:G颠换。
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Characterization of the recombinant MutY homolog, an adenine DNA glycosylase, from yeast Schizosaccharomyces pombe.来自粟酒裂殖酵母的腺嘌呤DNA糖基化酶——重组MutY同源物的特性分析。
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Cloning of a yeast 8-oxoguanine DNA glycosylase reveals the existence of a base-excision DNA-repair protein superfamily.酵母8-氧代鸟嘌呤DNA糖基化酶的克隆揭示了碱基切除DNA修复蛋白超家族的存在。
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