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Chromatin condensation and recruitment of PHD finger proteins to histone H3K4me3 are mutually exclusive.
Gatchalian, Jovylyn; Gallardo, Carmen Mora; Shinsky, Stephen A; Ospina, Ruben Rosas; Liendo, Andrea Mansilla; Krajewski, Krzysztof; Klein, Brianna J; Andrews, Forest H; Strahl, Brian D; M van Wely, Karel H; Kutateladze, Tatiana G.
Afiliación
  • Gatchalian J; Department of Pharmacology, University of Colorado School of Medicine, Aurora, CO 80045, USA.
  • Gallardo CM; Department of Immunology and Oncology, Centro Nacional de Biotecnología/CSIC, 28049 Madrid, Spain.
  • Shinsky SA; Department of Biochemistry & Biophysics, The University of North Carolina School of Medicine, Chapel Hill, NC 27599, USA.
  • Ospina RR; Department of Pharmacology, University of Colorado School of Medicine, Aurora, CO 80045, USA.
  • Liendo AM; Department of Immunology and Oncology, Centro Nacional de Biotecnología/CSIC, 28049 Madrid, Spain.
  • Krajewski K; Department of Biochemistry & Biophysics, The University of North Carolina School of Medicine, Chapel Hill, NC 27599, USA.
  • Klein BJ; Department of Pharmacology, University of Colorado School of Medicine, Aurora, CO 80045, USA.
  • Andrews FH; Department of Pharmacology, University of Colorado School of Medicine, Aurora, CO 80045, USA.
  • Strahl BD; Department of Biochemistry & Biophysics, The University of North Carolina School of Medicine, Chapel Hill, NC 27599, USA.
  • M van Wely KH; Department of Immunology and Oncology, Centro Nacional de Biotecnología/CSIC, 28049 Madrid, Spain kvanwely@cnb.csic.es.
  • Kutateladze TG; Department of Pharmacology, University of Colorado School of Medicine, Aurora, CO 80045, USA tatiana.kutateladze@ucdenver.edu.
Nucleic Acids Res ; 44(13): 6102-12, 2016 07 27.
Article en En | MEDLINE | ID: mdl-27016734
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.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Cromatina / Heterocromatina / Procesamiento Proteico-Postraduccional / Mitosis Idioma: En Revista: Nucleic Acids Res Año: 2016 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Cromatina / Heterocromatina / Procesamiento Proteico-Postraduccional / Mitosis Idioma: En Revista: Nucleic Acids Res Año: 2016 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido