English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
 Local TagsRelease HistoryDetailsSummary
  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.

Item is

 

show all hide all

Basic

show hide
Item Permalink: https://hdl.handle.net/21.11116/0000-0004-71F7-6 Version Permalink: https://hdl.handle.net/21.11116/0000-0004-7661-A
Genre: Journal Article

Files

show Files

Locators

show
hide
Locator:
https://www.ncbi.nlm.nih.gov/pubmed/30257210 (Any fulltext)
Description:
-
OA-Status:

Creators

show
hide
 Creators:
Bartlett, E.1, Author
Bonfiglio, J. J.1, Author
Prokhorova, E.1, Author
Colby, T.1, Author
Zobel, F.1, Author
Ahel, I.1, Author
Matic, I.1, Author
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              

Content

show
hide
Free keywords: DNA damage Hpf1 Parp1 histone code histone crosstalk nucleosome serine ADP-ribosylation tyrosine ADP-ribosylation
 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.

Details

show
hide
Language(s):
 Dates: 2018-09-252018
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: Other: 30257210
DOI: 10.1016/j.celrep.2018.08.092
ISSN: 2211-1247 (Electronic)
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Cell Rep
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 24 (13) Sequence Number: - Start / End Page: 3488 - 3502 e5 Identifier: -