极端耐辐射细菌耐辐射奇异球菌中氧化碱基的修复
Repair of oxidized bases in the extremely radiation-resistant bacterium Deinococcus radiodurans.
作者信息
Bauche C, Laval J
机构信息
Groupe "Réparation des Lésions Radio-et Chimio-Induites," UMR 1772 CNRS, Institut Gustave Roussy, 94805 Villejuif Cedex, France.
出版信息
J Bacteriol. 1999 Jan;181(1):262-9. doi: 10.1128/JB.181.1.262-269.1999.
Abstract
Deinococcus radiodurans is able to resist and survive extreme DNA damage induced by ionizing radiation and many other DNA-damaging agents. It is believed that it possesses highly efficient DNA repair mechanisms. To characterize the repair pathway of oxidized purines in this bacteria, we have purified, from crude extracts, proteins that recognize these oxidized bases. We report here that D. radiodurans possesses two proteins excising the oxidized purines (formamidopyrimidine and 8-oxoguanine) by a DNA glycosylase-a purinic/apyrimidine lyase mechanism. Moreover, one of those proteins is endowed with a thymine glycol DNA glycosylase activity. One of these proteins could be the homolog of the Escherichia coli Fpg enzyme, which confirms the existence of a base excision repair system in this bacteria.
摘要
耐辐射球菌能够抵抗并在电离辐射和许多其他DNA损伤剂诱导的极端DNA损伤中存活。据信它拥有高效的DNA修复机制。为了表征这种细菌中氧化嘌呤的修复途径，我们从粗提物中纯化了识别这些氧化碱基的蛋白质。我们在此报告，耐辐射球菌拥有两种通过DNA糖基化酶-嘌呤/嘧啶裂解酶机制切除氧化嘌呤（甲酰胺嘧啶和8-氧鸟嘌呤）的蛋白质。此外，其中一种蛋白质具有胸腺嘧啶乙二醇DNA糖基化酶活性。这些蛋白质之一可能是大肠杆菌Fpg酶的同源物，这证实了这种细菌中存在碱基切除修复系统。
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