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首页> 外文期刊>Biochemistry >Physical and Functional Interactions between 3-Methyladenine DNA Glycosylase and Topoisomerase I in Mycobacteria
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Physical and Functional Interactions between 3-Methyladenine DNA Glycosylase and Topoisomerase I in Mycobacteria

机译：3-甲基腺嘌呤DNA糖基化酶和拓扑异构酶I在分枝杆菌中的物理和功能相互作用。

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摘要

DNA glycosylases play important roles in DNA repair in a variety of organisms, including humans. However, the function and regulation of these enzymes in the pathogenic bacterium Mycobacterium tuberculosis and related species are poorly understood. In the present study, the physical and functional interactions between 3-methyladenine DNA glycosy-lase (MAG) and topoisomerase I (TopA) in M. tuberculosis and M. smegmatis were characterized. MAG was found to inhibit the function of TopA in relaxing supercoiled DNA. In contrast, TopA stimulated the cleavage function of MAG on a damaged DNA substrate that contains hypoxanthine. The interaction between the two proteins was conserved between the two mycobacterial species. Several mutations in MAG that led to the loss of its interaction with and activity regulation of TopA were also characterized. The results of this study further elucidate glycosylase regulation in both M. smegmatis and M. tuberculosis.
机译：DNA糖基化酶在包括人类在内的多种生物体的DNA修复中起着重要作用。然而，人们对病原菌结核分枝杆菌和相关物种中这些酶的功能和调控知之甚少。在本研究中，表征了3-甲基腺嘌呤DNA糖基化酶（MAG）和拓扑异构酶I（TopA）在结核分枝杆菌和耻垢分枝杆菌中的物理和功能相互作用。发现MAG抑制TopA在松弛超螺旋DNA中的功能。相反，TopA刺激了MAG在含有次黄嘌呤的受损DNA底物上的切割功能。两种蛋白质之间的相互作用在两种分枝杆菌物种之间是保守的。还表征了MAG中的几种突变，这些突变导致其与TopA的相互作用丧失和活性调节。这项研究的结果进一步阐明了耻垢分枝杆菌和结核分枝杆菌中的糖基化酶调控。

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