5-Hydroxymethyluracil-DNA glycosylase activity may be a differentiated mammalian function

R.J. Boorstein , D.D. Levy , G.W. Teebor
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引用次数: 44

Abstract

To determine the prevalance of the repaire enzyme HMU-DNA hlycosylase we assayed its activity in whole cell extracts of several bacterial species, the eukaryotic yeast Saccharomyces cerevesiae, mammalian cell line and murine tissue. Enzyme activity was constitutively present in murine, hasmter and human cell lines. It was not inducible by exposing cells to oxidative stress from ionizing radiation or by incubating cells with the 2′-deoxynucleoside of HMU, HMdU. In murine tissue, enzyme activity was highest in brain and thymus. HMU-DNA glycosylase activity was not detectable in bacteria or yeast nor could activity be detected after exposure of cells to H2O2. These results suggest that, in contrast to other DNA-repair enzymes, HMU-DNA glycosylase is a differentiated function limited to higher eukaryotic organisms.

5-羟甲基尿嘧啶- dna糖基化酶活性可能是一种分化的哺乳动物功能
为了确定修复酶HMU-DNA糖基化酶在几种细菌、真核酵母、哺乳动物细胞系和小鼠组织的全细胞提取物中的活性,我们对其进行了检测。酶活性在小鼠、仓鼠和人类细胞系中均存在。将细胞暴露于电离辐射的氧化应激或用HMU的2 ' -脱氧核苷,HMdU孵育细胞都不能诱导。在小鼠组织中,脑和胸腺的酶活性最高。细菌或酵母中未检测到HMU-DNA糖基酶活性,细胞暴露于H2O2后也无法检测到活性。这些结果表明,与其他dna修复酶相比,HMU-DNA糖基化酶是一种仅限于高等真核生物的分化功能。
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