Assembly of the base excision repair complex on abasic DNA and role of adenomatous polyposis coli on its functional activity.
Assembly of the base excision repair complex on abasic DNA and role of adenomatous polyposis coli on its functional activity.
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DOI：
10.1021/bi102000q
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发表时间：
2011-03-22
期刊：
影响因子：
2.9
通讯作者：
Narayan S
中科院分区：
文献类型：
--
作者：
Jaiswal AS;Narayan S
碱基切除修复(BER)蛋白在体内对基本DNA的组装和稳定性，以及腺瘤性息肉病(APC)蛋白在这一过程中的作用目前尚不清楚。我们研究了多蛋白BER复合体在基本DNA(F-DNA)上的组装，并表征了相关蛋白的物理和功能活性。我们发现，误码率复合体包含长斑块误码率系统的所有必要成分，如APE1、POL-β、FEN-1和DNA连接酶I。有趣的是，在误码率复合体中也存在野生型APC。BER蛋白在F-DNA上的组装动力学是快速的，并根据修复过程中的需要按顺序出现。BER复合体中野生型APC的存在导致BER蛋白组装减少，并对长斑块BER产生负面影响。这些结果表明，该复合体中的主要BER蛋白组装在F-DNA上，并能够进行DNA修复。BER复合体中的野生型APC减少了修复活动，可能是由于与系统的多个组件相互作用。
Assembly and stability of base excision repair (BER) proteins in vivo onto abasic DNA and the role of adenomatous polyposis coli (APC) protein in this process is currently unclear. We have studied the assembly of a multiprotein BER complex onto abasic DNA (F-DNA) and characterized the physical and functional activity of the associated proteins. We found that the BER complex contained all the essential components of the Long-patch BER system, such as APE1, Pol-β, Fen-1 and DNA ligase I. Interestingly, wild-type APC was also present in the BER complex. Kinetics of the assembly of BER proteins onto the F-DNA were rapid and appeared in sequential order depending upon their requirement in the repair process. Presence of wild-type APC in the BER complex caused a decrease in the assembly of BER proteins and negatively affected long-patch BER. These results suggest that major BER proteins in the complex are assembled onto F-DNA, and are competent in performing DNA repair. Wild-type APC in the BER complex reduces the repair activity, probably, due to interaction with multiple components of the system.
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