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Structural basis of nucleosome transcription mediated by Chd1 and FACT

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Farnung,  L.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Ochmann,  M.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Engeholm,  M.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Cramer,  P.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Citation

Farnung, L., Ochmann, M., Engeholm, M., & Cramer, P. (2021). Structural basis of nucleosome transcription mediated by Chd1 and FACT. Nature Structural and Molecular Biology, 28(4), 382-387. doi:10.1038/s41594-021-00578-6.


Cite as: http://hdl.handle.net/21.11116/0000-0008-5501-7
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.