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  Interplay of Histone Marks with Serine ADP-Ribosylation

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.

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Datensatz-Permalink: https://hdl.handle.net/21.11116/0000-0004-71F7-6 Versions-Permalink: https://hdl.handle.net/21.11116/0000-0004-7661-A
Genre: Zeitschriftenartikel

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externe Referenz:
https://www.ncbi.nlm.nih.gov/pubmed/30257210 (beliebiger Volltext)
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 Urheber:
Bartlett, E.1, Autor
Bonfiglio, J. J.1, Autor
Prokhorova, E.1, Autor
Colby, T.1, Autor
Zobel, F.1, Autor
Ahel, I.1, Autor
Matic, I.1, Autor
Affiliations:
1Matic – Proteomics of post-translational modifications, Research Groups, Max Planck Institute for Biology of Ageing, Max Planck Society, Joseph-Stelzmann-Str. 9b, D-50931 Cologne, DE, ou_1942299              

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Schlagwörter: DNA damage Hpf1 Parp1 histone code histone crosstalk nucleosome serine ADP-ribosylation tyrosine ADP-ribosylation
 Zusammenfassung: 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.

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 Datum: 2018-09-252018
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: Anderer: 30257210
DOI: 10.1016/j.celrep.2018.08.092
ISSN: 2211-1247 (Electronic)
 Art des Abschluß: -

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Titel: Cell Rep
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 24 (13) Artikelnummer: - Start- / Endseite: 3488 - 3502 e5 Identifikator: -