Header

UZH-Logo

Maintenance Infos

ADP-ribosylation of histones by ARTD1: an additional module of the histone code?


Hottiger, M O (2011). ADP-ribosylation of histones by ARTD1: an additional module of the histone code? FEBS Letters, 585(11):1595-1599.

Abstract

ADP-ribosylation is a covalent post-translational protein modification catalyzed by ADP-ribosyltransferases and is involved in important processes such as cell cycle regulation, DNA damage response, replication or transcription. Histones are ADP-ribosylated by ADP-ribosyltransferase diphtheria toxin-like 1 at specific amino acid residues, in particular lysines, of the histones tails. Specific ADP-ribosyl hydrolases and poly-ADP-ribose glucohydrolases degrade the ADP-ribose polymers. The ADP-ribose modification is read by zinc finger motifs or macrodomains, which then regulate chromatin structure and transcription. Thus, histone ADP-ribosylation may be considered an additional component of the histone code.

Abstract

ADP-ribosylation is a covalent post-translational protein modification catalyzed by ADP-ribosyltransferases and is involved in important processes such as cell cycle regulation, DNA damage response, replication or transcription. Histones are ADP-ribosylated by ADP-ribosyltransferase diphtheria toxin-like 1 at specific amino acid residues, in particular lysines, of the histones tails. Specific ADP-ribosyl hydrolases and poly-ADP-ribose glucohydrolases degrade the ADP-ribose polymers. The ADP-ribose modification is read by zinc finger motifs or macrodomains, which then regulate chromatin structure and transcription. Thus, histone ADP-ribosylation may be considered an additional component of the histone code.

Statistics

Citations

27 citations in Web of Science®
30 citations in Scopus®
Google Scholar™

Altmetrics

Downloads

1 download since deposited on 28 Feb 2012
0 downloads since 12 months
Detailed statistics

Additional indexing

Item Type:Journal Article, refereed, further contribution
Communities & Collections:05 Vetsuisse Faculty > Department of Molecular Mechanisms of Disease
07 Faculty of Science > Department of Molecular Mechanisms of Disease
Dewey Decimal Classification:570 Life sciences; biology
Language:English
Date:2011
Deposited On:28 Feb 2012 12:58
Last Modified:05 Apr 2016 15:28
Publisher:Elsevier
ISSN:0014-5793
Publisher DOI:https://doi.org/10.1016/j.febslet.2011.03.031
PubMed ID:21420964

Download