Interplay of Histone Marks with Serine ADP-Ribosylation

Bartlett, E.; Bonfiglio, J. J.; Prokhorova, E.; Colby, T.; Zobel, F.; Ahel, I.; Matic, I.

doi:10.1016/j.celrep.2018.08.092

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Interplay of Histone Marks with Serine ADP-Ribosylation

MPS-Authors

Bartlett, E.
Matic – Proteomics of post-translational modifications, Research Groups, Max Planck Institute for Biology of Ageing, Max Planck Society;

Bonfiglio, J. J.
Matic – Proteomics of post-translational modifications, Research Groups, Max Planck Institute for Biology of Ageing, Max Planck Society;

Prokhorova, E.
Matic – Proteomics of post-translational modifications, Research Groups, Max Planck Institute for Biology of Ageing, Max Planck Society;

Colby, T.
Matic – Proteomics of post-translational modifications, Research Groups, Max Planck Institute for Biology of Ageing, Max Planck Society;

Zobel, F.
Matic – Proteomics of post-translational modifications, Research Groups, Max Planck Institute for Biology of Ageing, Max Planck Society;

Ahel, I.
Matic – Proteomics of post-translational modifications, Research Groups, Max Planck Institute for Biology of Ageing, Max Planck Society;

Matic, I.
Matic – Proteomics of post-translational modifications, Research Groups, Max Planck Institute for Biology of Ageing, Max Planck Society;

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https://www.ncbi.nlm.nih.gov/pubmed/30257210
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Citation

Bartlett, E., Bonfiglio, J. J., Prokhorova, E., Colby, T., Zobel, F., Ahel, I., et al. (2018). Interplay of Histone Marks with Serine ADP-Ribosylation. Cell Rep, 24(13), 3488-3502 e5. doi:10.1016/j.celrep.2018.08.092.

Cite as: https://hdl.handle.net/21.11116/0000-0004-71F7-6

Abstract

Serine ADP-ribosylation (Ser-ADPr) is a recently discovered protein modification that is catalyzed by PARP1 and PARP2 when in complex with the eponymous histone PARylation factor 1 (HPF1). In addition to numerous other targets, core histone tails are primary acceptors of Ser-ADPr in the DNA damage response. Here, we show that specific canonical histone marks interfere with Ser-ADPr of neighboring residues and vice versa. Most notably, acetylation, but not methylation of H3K9, is mutually exclusive with ADPr of H3S10 in vitro and in vivo. We also broaden the O-linked ADPr spectrum by providing evidence for tyrosine ADPr on HPF1 and other proteins. Finally, we facilitate wider investigations into the interplay of histone marks with Ser-ADPr by introducing a simple approach for profiling posttranslationally modified peptides. Our findings implicate Ser-ADPr as a dynamic addition to the complex interplay of modifications that shape the histone code.