Structural basis of nucleosome transcription mediated by Chd1 and FACT

IF 16.8 1区 生物学
L. Farnung, M. Ochmann, M. Engeholm, P. Cramer
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引用次数: 55

Abstract

Efficient transcription of RNA polymerase II (Pol II) through nucleosomes requires the help of various factors. Here we show biochemically that Pol II transcription through a nucleosome is facilitated by the chromatin remodeler Chd1 and the histone chaperone FACT when the elongation factors Spt4/5 and TFIIS are present. We report cryo-EM structures of transcribing Saccharomyces cerevisiae Pol II−Spt4/5−nucleosome complexes with bound Chd1 or FACT. In the first structure, Pol II transcription exposes the proximal histone H2A−H2B dimer that is bound by Spt5. Pol II has also released the inhibitory DNA-binding region of Chd1 that is poised to pump DNA toward Pol II. In the second structure, Pol II has generated a partially unraveled nucleosome that binds FACT, which excludes Chd1 and Spt5. These results suggest that Pol II progression through a nucleosome activates Chd1, enables FACT binding and eventually triggers transfer of FACT together with histones to upstream DNA. Structural and functional analyses of RNA polymerase II−nucleosome complexes reveal how the chromatin remodeler Chd1 and the histone chaperone FACT mediate Pol II transcription through a nucleosome.
Chd1和FACT介导核小体转录的结构基础
RNA聚合酶II(Pol II)通过核小体的有效转录需要各种因素的帮助。在这里,我们从生物化学角度表明,当存在延伸因子Spt4/5和TFIIS时,染色质重塑因子Chd1和组蛋白伴侣FACT促进了Pol II通过核小体的转录。我们报道了转录酿酒酵母Pol II−Spt4/5−核小体复合物与结合的Chd1或FACT的冷冻电镜结构。在第一个结构中,Pol II转录暴露了与Spt5结合的近端组蛋白H2A−H2B二聚体。Pol II还释放了Chd1的抑制性DNA结合区,该区准备将DNA泵送到Pol II。在第二种结构中,Pol II产生了一个部分解开的核小体,它结合FACT,不包括Chd1和Spt5。这些结果表明,Pol II通过核小体的进展激活了Chd1,使FACT结合,并最终触发FACT与组蛋白一起转移到上游DNA。RNA聚合酶II-核小体复合物的结构和功能分析揭示了染色质重塑因子Chd1和组蛋白伴侣FACT如何通过核小体介导Pol II转录。
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来源期刊
Nature Structural &Molecular Biology
Nature Structural &Molecular Biology 生物-生化与分子生物学
自引率
1.80%
发文量
160
期刊介绍: Nature Structural & Molecular Biology is a monthly journal that focuses on the functional and mechanistic understanding of how molecular components in a biological process work together. It serves as an integrated forum for structural and molecular studies. The journal places a strong emphasis on the functional and mechanistic understanding of how molecular components in a biological process work together. Some specific areas of interest include the structure and function of proteins, nucleic acids, and other macromolecules, DNA replication, repair and recombination, transcription, regulation of transcription and translation, protein folding, processing and degradation, signal transduction, and intracellular signaling.
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