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Journal Article

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

MPS-Authors
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Wang,  H.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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

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Dienemann,  C.
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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Fulltext (public)

3181797.pdf
(Preprint), 9MB

Supplementary Material (public)

3181797_Suppl_1.pdf
(Supplementary material), 3MB

3181797_Suppl_2.pdf
(Supplementary material), 2MB

3181797_Suppl_3.pdf
(Supplementary material), 27KB

Citation

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


Cite as: https://hdl.handle.net/21.11116/0000-0005-58E9-2
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.