| Literature DB >> 27016734 |
Jovylyn Gatchalian1, Carmen Mora Gallardo2, Stephen A Shinsky3, Ruben Rosas Ospina1, Andrea Mansilla Liendo2, Krzysztof Krajewski3, Brianna J Klein1, Forest H Andrews1, Brian D Strahl3, Karel H M van Wely4, Tatiana G Kutateladze5.
Abstract
Histone post-translational modifications, and specific combinations they create, mediate a wide range of nuclear events. However, the mechanistic bases for recognition of these combinations have not been elucidated. Here, we characterize crosstalk between H3T3 and H3T6 phosphorylation, occurring in mitosis, and H3K4me3, a mark associated with active transcription. We detail the molecular mechanisms by which H3T3ph/K4me3/T6ph switches mediate activities of H3K4me3-binding proteins, including those containing plant homeodomain (PHD) and double Tudor reader domains. Our results derived from nuclear magnetic resonance chemical shift perturbation analysis, orthogonal binding assays and cell fluorescence microscopy studies reveal a strong anti-correlation between histone H3T3/T6 phosphorylation and retention of PHD finger proteins in chromatin during mitosis. Together, our findings uncover the mechanistic rules of chromatin engagement for H3K4me3-specific readers during cell division.Entities:
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Year: 2016 PMID： 27016734 PMCID： PMC5291243 DOI： 10.1093/nar/gkw193
Source DB: PubMed Journal: Nucleic Acids Res ISSN： 0305-1048 Impact factor: 16.971