SWI2/SNF2 CHROMATIN-REMODELING DOMAIN OF EUKARYOTIC RAD54

这个子项目是许多利用 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 SWI 2/SNF 2染色质重塑蛋白介导核小体和其他DNA相关蛋白的动员。SWI 2/SNF 2蛋白含有SF 2解旋酶特征性的序列基序，但不具有解旋酶活性。相反，它们将ATP水解与DNA中超螺旋扭转的产生结合起来。斑马鱼Rad 54的核小体重塑结构域的结构，一种参与Rad 51介导的同源重组的蛋白质，揭示了SWI 2/SNF 2酶的核心由两个类似于SF 2解旋酶的α/β-叶组成。Rad 54解旋酶叶含有形成两个螺旋结构域的插入物，每个叶内一个。这些插入包含SWI 2/SNF 2特异性序列基序，可能是SWI 2/SNF 2功能的核心。由两个裂片形成的宽裂缝，两侧是螺旋插入物，包含SWI 2/SNF 2蛋白中保守的残基和SF 2解旋酶与DNA结合相关的基序。Rad 54结构表明SWI 2/SNF 2蛋白使用类似于解旋酶的机制在dsDNA上移位。 这项工作发表在Nature Structural Molecular Biology上，结构存放在PDB（1 Z3 I）中。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. SWI2/SNF2 chromatin-remodeling proteins mediate the mobilization of nucleosomes and other DNA-associated proteins. SWI2/SNF2 proteins contain sequence motifs characteristic of SF2 helicases but do not have helicase activity. Instead, they couple ATP hydrolysis with the generation of superhelical torsion in DNA. The structure of the nucleosome-remodeling domain of zebrafish Rad54, a protein involved in Rad51-mediated homologous recombination, reveals that the core of the SWI2/SNF2 enzymes consist of two alpha/beta-lobes similar to SF2 helicases. The Rad54 helicase lobes contain insertions that form two helical domains, one within each lobe. These insertions contain SWI2/SNF2-specific sequence motifs likely to be central to SWI2/SNF2 function. A broad cleft formed by the two lobes and flanked by the helical insertions contains residues conserved in SWI2/SNF2 proteins and motifs implicated in DNA-binding by SF2 helicases. The Rad54 structure suggests that SWI2/SNF2 proteins use a mechanism analogous to helicases to translocate on dsDNA. This work was published in Nature Structural Molecular Biology and the structure deposited in the PDB (1Z3I).