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Serine is a new target residue for endogenous ADP-ribosylation on histones

Nature Chemical Biology volume 12, pages 998–1000 (2016)Cite this article

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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.

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Figure 1: Partial FASP method for increased sequence coverage of histones.
Figure 2: Identification of histone ADPr marks.
Figure 3: Modulation of serine ADPr marks on core histones after DNA damage.

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Acknowledgements

Many thanks to A. Zhiteneva, W. Earnshaw (University of Edinburgh) and M. Tatham (University of Dundee) for comments on the manuscript. Chicken bursal lymphoma DT40 cells were a gift from W. Earnshaw (Wellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh, UK). pGEX-4T1 GST-PARP10cd plasmid was a gift from B. Lüscher (Department of Biochemistry and Molecular Biology, RWTH Aachen University, Aachen, Germany). This work was funded by Deutsche Forschungsgemeinschaft (Cellular Stress Responses in Aging-Associated Diseases) (grant EXC 229 to I.M.) and the European Union's Horizon 2020 research and innovation program (Marie Sklodowska-Curie grant agreement no. 657501 to J.J.B. and I.M.). The work in the Ahel laboratory is funded by the Wellcome Trust (grant 101794) and the European Research Council (grant 281739).

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Author notes

  1. Orsolya Leidecker and Juan José Bonfiglio: These authors contributed equally to this work.

Authors and Affiliations

  1. Max Planck Institute for Biology of Ageing, Cologne, Germany

    Orsolya Leidecker, Juan José Bonfiglio, Thomas Colby, Qi Zhang, Ilian Atanassov, Anna Stockum & Ivan Matic

  2. Sir William Dunn School of Pathology, University of Oxford, Oxford, UK

    Roko Zaja, Luca Palazzo & Ivan Ahel

Authors
  1. Orsolya Leidecker
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  2. Juan José Bonfiglio
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  4. Qi Zhang
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  8. Anna Stockum
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  9. Ivan Ahel
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Contributions

I.M., O.L. and J.J.B. designed research. O.L. and J.J.B. performed experiments and acquired and analyzed MS data. T.C. optimized MS methods and contributed to the acquisition and analysis of MS data. Q.Z. performed histone purification and digestion experiments. I. Atanassov performed bioinformatics analyses. A.S. performed immuno-slot blot experiments. L.P. and R.Z. performed protein purification and in vitro assays. I. Ahel and R.Z. contributed to the histone purification experiments and supporting studies. I.M. analyzed data and wrote the manuscript.

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Correspondence to Ivan Matic.

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The authors declare no competing financial interests.

Supplementary information

Supplementary Text and Figures

Supplementary Results, Supplementary Figures 1–11, Supplementary Tables 1–2 and Supplementary Note. (PDF 16867 kb)

Supplementary Dataset 1

SILAC-based quantification of histone marks: DNA damage and olaparib experiments. (XLSX 69 kb)

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Leidecker, O., Bonfiglio, J., Colby, T. et al. Serine is a new target residue for endogenous ADP-ribosylation on histones. Nat Chem Biol 12, 998–1000 (2016). https://doi.org/10.1038/nchembio.2180

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