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Serine is a new target residue for endogenous ADP-ribosylation on histones.
Leidecker, Orsolya; Bonfiglio, Juan José; Colby, Thomas; Zhang, Qi; Atanassov, Ilian; Zaja, Roko; Palazzo, Luca; Stockum, Anna; Ahel, Ivan; Matic, Ivan.
Afiliação
  • Leidecker O; Max Planck Institute for Biology of Ageing, Joseph-Stelzmann-Strasse 9b, Cologne 50931, Germany.
  • Bonfiglio JJ; Max Planck Institute for Biology of Ageing, Joseph-Stelzmann-Strasse 9b, Cologne 50931, Germany.
  • Colby T; Max Planck Institute for Biology of Ageing, Joseph-Stelzmann-Strasse 9b, Cologne 50931, Germany.
  • Zhang Q; Max Planck Institute for Biology of Ageing, Joseph-Stelzmann-Strasse 9b, Cologne 50931, Germany.
  • Atanassov I; Max Planck Institute for Biology of Ageing, Joseph-Stelzmann-Strasse 9b, Cologne 50931, Germany.
  • Zaja R; Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford, OX1 3RE, UK.
  • Palazzo L; Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford, OX1 3RE, UK.
  • Stockum A; Max Planck Institute for Biology of Ageing, Joseph-Stelzmann-Strasse 9b, Cologne 50931, Germany.
  • Ahel I; Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford, OX1 3RE, UK.
  • Matic I; Max Planck Institute for Biology of Ageing, Joseph-Stelzmann-Strasse 9b, Cologne 50931, Germany.
Nat Chem Biol ; 12(12): 998-1000, 2016 Dec.
Article em En | MEDLINE | ID: mdl-27723750
ABSTRACT
ADP-ribosylation (ADPr) is a biologically and clinically important post-translational modification, but little is known about the amino acids it targets on cellular proteins. Here we present a proteomic approach for direct in vivo identification and quantification of ADPr sites on histones. We have identified 12 unique ADPr sites in human osteosarcoma cells and report serine ADPr as a new type of histone mark that responds to DNA damage.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Serina / Histonas / Difosfato de Adenosina / Processamento de Proteína Pós-Traducional Limite: Humans Idioma: En Ano de publicação: 2016 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Serina / Histonas / Difosfato de Adenosina / Processamento de Proteína Pós-Traducional Limite: Humans Idioma: En Ano de publicação: 2016 Tipo de documento: Article