Xiao H, Sandaltzopoulos R, Wang H M, Hamiche A, Ranallo R, Lee K M, Fu D, Wu C
Laboratory of Molecular Cell Biology, National Cancer Institute, Building 37, Room 6068, National Institutes of Health, Bethesda, MD 20892, USA.
Mol Cell. 2001 Sep;8(3):531-43. doi: 10.1016/s1097-2765(01)00345-8.
NURF is an ISWI complex of four proteins that uses the energy of ATP hydrolysis to catalyze nucleosome sliding. Three NURF components have been identified previously. We have cloned cDNA encoding the largest NURF subunit, revealing a 301 kDa polypeptide (NURF301) that shares structural motifs with ACF1. We have reconstituted full and partial NURF complexes from recombinant proteins and show that NURF301 and the ISWI ATPase are necessary and sufficient for accurate and efficient nucleosome sliding. An HMGA/HMGI(Y)-like domain of NURF301 that facilitates nucleosome sliding indicates the importance of DNA conformational changes in the sliding mechanism. NURF301 also shows interactions with sequence-specific transcription factors, providing a basis for targeted recruitment of the NURF complex to specific genes.
NURF是一种由四种蛋白质组成的ISWI复合物，它利用ATP水解的能量来催化核小体滑动。此前已鉴定出三种NURF组分。我们克隆了编码最大NURF亚基的cDNA，揭示了一种301 kDa的多肽（NURF301），它与ACF1共享结构基序。我们已经用重组蛋白重建了完整和部分NURF复合物，并表明NURF301和ISWI ATP酶对于准确和高效的核小体滑动是必要且充分的。NURF301的一个HMGA/HMGI(Y)样结构域促进了核小体滑动，这表明DNA构象变化在滑动机制中的重要性。NURF301还显示出与序列特异性转录因子的相互作用，为将NURF复合物靶向募集到特定基因提供了基础。
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