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首页> 外文会议>ASMS Conference on Mass Spectrometry and Allied Topics >DNA-MEDIATED REF1 CONFORMATIONAL CHANGES: POSSIBLE MECHANISM FOR PROTEIN RECRUITMENT IN BASE EXCISION REPAIR (BER) PATHWAY
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DNA-MEDIATED REF1 CONFORMATIONAL CHANGES: POSSIBLE MECHANISM FOR PROTEIN RECRUITMENT IN BASE EXCISION REPAIR (BER) PATHWAY

机译：DNA介导的REF1一致性变化：基础切除修复（BER）途径中蛋白质招募的可能机制

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摘要

Abasic (AP) sites are the most common mutagenic lesions arising in genomic DNA. Recognition of an abasic site by Ape1 (apurinic/apyrimidinic endonucleases) initiates DNA repair, subsequently cleaving the backbone 5' to the AP site. Fluorescence, CD, and protein footprinting show that Ape1 undergoes conformational changes during recognition, incision, and post-incision interactions with DNA. Conformational changes have been localized to the Ref1 domain and may act as a structural trigger to recruit downstream proteins into the pathway. Although Ape1 and Pol(beta) (DNA Polymerase beta) interactions have been reported in yeast-two hybrid interactions, pull-down, and band-shift assays, specific residue contact information is lacking. We are employing footprinting and site-specific photo crosslinking with mass spectrometric analysis to determine residues engaged in protein-protein interactions.
机译：Abasic（AP）位点是基因组DNA中最常见的致突变性病变。识别APE1（茴香/亚嘌呤蛋白内切核酸酶）引发DNA修复，随后将骨干5'切割到AP位点。荧光，CD和蛋白质足迹表明，APE1在识别，切口和切口后与DNA相互作用期间经历一致性变化。构象变化已经定位到REF1结构域，可以作为结构触发，以将下游蛋白募集到途径中。尽管在酵母 - 两个杂交相互作用，下拉和带移测定中报道了APE1和POL（β）（DNA聚合酶β）相互作用，但缺乏特定的残留率接触信息。我们正在采用具有质谱分析的脚印和特异性照片交联，以确定从事蛋白质 - 蛋白质相互作用的残留物。

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