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  Structure of H3K36-methylated nucleosome-PWWP complex reveals multivalent cross-gyre binding.

Wang, H., Farnung, L., Dienemann, C., & Cramer, P. (2020). Structure of H3K36-methylated nucleosome-PWWP complex reveals multivalent cross-gyre binding. Nature Structural and Molecular Biology, 27(1), 8-13. doi:10.1038/s41594-019-0345-4.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0005-58E9-2 Version Permalink: http://hdl.handle.net/21.11116/0000-0005-F411-4
Genre: Journal Article

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 Creators:
Wang, H.1, Author              
Farnung, L.1, Author              
Dienemann, C.1, Author              
Cramer, P.1, Author              
Affiliations:
1Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1863498              

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 Abstract: Recognition of histone-modified nucleosomes by specific reader domains underlies the regulation of chromatin-associated processes. Whereas structural studies revealed how reader domains bind modified histone peptides, it is unclear how reader domains interact with modified nucleosomes. Here, we report the cryo-electron microscopy structure of the PWWP reader domain of human transcriptional coactivator LEDGF in complex with an H3K36-methylated nucleosome at 3.2-Å resolution. The structure reveals multivalent binding of the reader domain to the methylated histone tail and to both gyres of nucleosomal DNA, explaining the known cooperative interactions. The observed cross-gyre binding may contribute to nucleosome integrity during transcription. The structure also explains how human PWWP domain-containing proteins are recruited to H3K36-methylated regions of the genome for transcription, histone acetylation and methylation, and for DNA methylation and repair.

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Language(s): eng - English
 Dates: 2019-12-092020-01
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/s41594-019-0345-4
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Title: Nature Structural and Molecular Biology
Source Genre: Journal
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Pages: - Volume / Issue: 27 (1) Sequence Number: - Start / End Page: 8 - 13 Identifier: -