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Recognition of mono-ADP-ribosylated ARTD10 substrates by ARTD8 macrodomains

Forst, Alexandra H ; Karlberg, Tobias LU ; Herzog, Nicolas ; Thorsell, Ann-Gerd ; Gross, Annika ; Feijs, Karla L H ; Verheugd, Patricia ; Kursula, Petri ; Nijmeijer, Bianca and Kremmer, Elisabeth , et al. (2013) In Structure 21(3). p.75-462
Abstract

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... (More)

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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publishing date
type
Contribution to journal
publication status
published
keywords
ADP Ribose Transferases/chemistry, Adenosine Diphosphate Ribose/chemistry, Animals, Binding Sites, Crystallography, X-Ray, Escherichia coli/genetics, HEK293 Cells, Histones/chemistry, Humans, Isoenzymes/chemistry, Kinetics, Mice, Molecular Docking Simulation, Molecular Dynamics Simulation, Mutation, Protein Binding, Protein Interaction Domains and Motifs, Protein Structure, Secondary, Recombinant Proteins/chemistry, Structure-Activity Relationship, Thermodynamics, ran GTP-Binding Protein/chemistry
in
Structure
volume
21
issue
3
pages
14 pages
publisher
Cell Press
external identifiers
  • scopus:84874456032
  • pmid:23473667
ISSN
0969-2126
DOI
10.1016/j.str.2012.12.019
language
English
LU publication?
no
additional info
Copyright © 2013 Elsevier Ltd. All rights reserved.
id
e7d93a50-7fcf-49d4-a828-76b40bb42f34
date added to LUP
2024-11-21 17:56:59
date last changed
2025-07-05 12:28:15
@article{e7d93a50-7fcf-49d4-a828-76b40bb42f34,
  abstract     = {{<p>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.</p>}},
  author       = {{Forst, Alexandra H and Karlberg, Tobias and Herzog, Nicolas and Thorsell, Ann-Gerd and Gross, Annika and Feijs, Karla L H and Verheugd, Patricia and Kursula, Petri and Nijmeijer, Bianca and Kremmer, Elisabeth and Kleine, Henning and Ladurner, Andreas G and Schüler, Herwig and Lüscher, Bernhard}},
  issn         = {{0969-2126}},
  keywords     = {{ADP Ribose Transferases/chemistry; Adenosine Diphosphate Ribose/chemistry; Animals; Binding Sites; Crystallography, X-Ray; Escherichia coli/genetics; HEK293 Cells; Histones/chemistry; Humans; Isoenzymes/chemistry; Kinetics; Mice; Molecular Docking Simulation; Molecular Dynamics Simulation; Mutation; Protein Binding; Protein Interaction Domains and Motifs; Protein Structure, Secondary; Recombinant Proteins/chemistry; Structure-Activity Relationship; Thermodynamics; ran GTP-Binding Protein/chemistry}},
  language     = {{eng}},
  month        = {{03}},
  number       = {{3}},
  pages        = {{75--462}},
  publisher    = {{Cell Press}},
  series       = {{Structure}},
  title        = {{Recognition of mono-ADP-ribosylated ARTD10 substrates by ARTD8 macrodomains}},
  url          = {{http://dx.doi.org/10.1016/j.str.2012.12.019}},
  doi          = {{10.1016/j.str.2012.12.019}},
  volume       = {{21}},
  year         = {{2013}},
}