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Identification of ADP-ribosylated peptides and ADP-ribose acceptor sites.

  • Rosenthal F Institute of Veterinary Biochemistry and Molecular Biology, University of Zurich, Switzerland.
  • Hottiger MO Institute of Veterinary Biochemistry and Molecular Biology, University of Zurich, Switzerland.
  • 2014-06-05
Published in:
  • Frontiers in bioscience (Landmark edition). - 2014
ADP Ribose Transferases
Adenosine Diphosphate Ribose
Amino Acids
Binding Sites
Humans
N-Glycosyl Hydrolases
NAD
Peptides
Protein Processing, Post-Translational
Proteins
English ADP-ribosylation is a post-translational modification of proteins that comprises the transfer of the ADP-ribose moiety from NAD+ to specific amino acid residues on substrate proteins or to ADP-ribose itself. It is catalyzed by ADP-ribosyltransferases, a family of currently 22 human proteins that all possess an ADP-ribosyltransferase catalytic domain. ADP-ribosylation is a reversible modification that can be hydrolyzed by ADP-ribosylhydrolases. In order to define the functional role of cellular ADP-ribosylation and the functional contribution of distinct ARTD family members, it is necessary to identify all ADP-ribosylated proteins, as well as their modified residues in the context of different cellular conditions and stresses. Here, we summarize the most recent progress in defining the cellular ADP-ribosylome and the efforts to detect ADP-ribose acceptor sites by enzymatic reactions and mass-spectrometry.
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  • English
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green
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https://sonar.ch/global/documents/147214
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