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TitleStructure of H3K36-methylated nucleosome-PWWP complex reveals multivalent cross-gyre binding.
Journal, issue, pagesNat Struct Mol Biol, Vol. 27, Issue 1, Page 8-13, Year 2020
Publish dateDec 9, 2019
AuthorsHaibo Wang / Lucas Farnung / Christian Dienemann / Patrick Cramer /
PubMed AbstractRecognition of histone-modified nucleosomes by specific reader domains underlies the regulation of chromatin-associated processes. Whereas structural studies revealed how reader domains bind modified ...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.
External linksNat Struct Mol Biol / PubMed:31819277 / PubMed Central
MethodsEM (single particle)
Resolution3.2 Å
Structure data

10069

6s01

EMDB-10069, PDB-6s01:
Structure of LEDGF PWWP domain bound H3K36 methylated nucleosome
Method: EM (single particle) / Resolution: 3.2 Å

Source
  • xenopus laevis (African clawed frog)
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsTRANSCRIPTION / LEDGF / PWWP / H3K36me3 / nucleosome

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