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Open Access Green as soon as Postprint is submitted to ZB.
Recognition of mono-ADP-ribosylated ARTD10 substrates by ARTD8 macrodomains.
Structure 21, 462-475 (2013)
ADP-ribosyltransferases (ARTs) catalyze the transfer of ADP-ribose from NAD(+) onto substrates. Some ARTs generate in an iterative process ADP-ribose polymers that serve as adaptors for distinct protein domains. Other ARTs, exemplified by ARTD10, function as mono-ADP-ribosyltransferases, but it has been unclear whether this modification occurs in cells and how it is read. We observed that ARTD10 colocalized with ARTD8 and defined its macrodomains 2 and 3 as readers of mono-ADP-ribosylation both in vitro and in cells. The crystal structures of these two ARTD8 macrodomains and isothermal titration calorimetry confirmed their interaction with ADP-ribose. These macrodomains recognized mono-ADP-ribosylated ARTD10, but not poly-ADP-ribosylated ARTD1. This distinguished them from the macrodomain of macroH2A1.1, which interacted with poly- but not mono-ADP-ribosylated substrates. Moreover, Ran, an ARTD10 substrate, was also read by ARTD8 macrodomains. This identifies readers of mono-ADP-ribosylated proteins, defines their structures, and demonstrates the presence of this modification in cells.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Polymerase-activity ; Dna-damage ; Poly(adp-ribose) ; Proteins ; Domains ; Binding ; Mechanism ; Chromatin ; Parp1 ; Ubiquitination
ISSN (print) / ISBN
0969-2126
e-ISSN
1878-4186
Journal
Structure
Quellenangaben
Volume: 21,
Issue: 3,
Pages: 462-475
Publisher
Cell Press
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Molecular Immunology (IMI)