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首页> 外文期刊>Biochemistry >Structural basis of DNA bridging by barrier-to-autointegration factor.
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Structural basis of DNA bridging by barrier-to-autointegration factor.

机译：通过障碍自整合因子桥接DNA的结构基础。

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摘要

Barrier-to-autointegration factor (BAF) is a host cell protein that plays a crucial role in retroviral integration. Preintegration complexes (PICs) stripped of BAF lose their normal integration activity, which can be restored by incubation with purified BAF. BAF bridges double-stranded DNA both intra- and intermolecularly in a non-sequence-specific manner, leading to the formation of a nucleoprotein network. BAF also binds to the nuclear protein lamina-associated polypeptide 2 (LAP2), and is localized with chromatin during interphase and mitosis. The crystal structure of homodimeric human BAF has been determined to 1.9 A resolution. The fold of the BAF monomer resembles that of the second domain of RuvA. This comparison revealed the presence of the helix-hairpin-helix (HhH) nonspecific DNA binding motif within BAF. A novel feature of BAF's HhH motif is the occupation of the metal binding site by the epsilon-amino group of Lys 6, providing an alternative means of sequestering positive charge. Mutational analysis corroborates the HhH motif's prominent role in DNA binding and argues against a previously proposed helix-turn-helix (HTH) binding site located in another region of the monomer. A model of BAF bridging DNA via the HhH motif is proposed.
机译：自动整合障碍因子（BAF）是一种宿主细胞蛋白，在逆转录病毒整合中起着至关重要的作用。去除BAF的预整合复合物（PIC）失去了正常的整合活性，可以通过与纯化的BAF孵育来恢复。 BAF以非序列特异性方式在分子内和分子间桥接双链DNA，导致形成核蛋白网络。 BAF还与核蛋白层相关多肽2（LAP2）结合，并在相间和有丝分裂期间定位于染色质。已确定同二聚体人BAF的晶体结构为1.9 A分辨率。 BAF单体的折叠类似于RuvA的第二个域。该比较揭示了BAF内存在螺旋-发夹-螺旋（HhH）非特异性DNA结合基序的存在。 BAF的HhH基序的一个新颖特征是Lys 6的ε-氨基占据了金属结合位点，提供了隔离正电荷的另一种方法。突变分析证实了HhH基序在DNA结合中的重要作用，并反对了先前提出的位于单体另一区域的螺旋-转-螺旋（HTH）结合位点。提出了通过HhH基序桥接DNA的BAF模型。

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