Abstract
ADP-ribosylation is a well-known post-translational protein modification, which regulates a variety of cellular processes. The proteins able to catalyze mono- or poly ADP-ribosylation of proteins belong to the family of ADP-ribosyltransferases. A variety of nuclear proteins has been described to be ADP-ribosylated, including ARTD1 itself and histone proteins. Despite intensive research during the last 40 years, the acceptor amino acids in ARTD1 or histone proteins could be identified and confirmed only recently by MS/MS and by site-directed mutagenesis. The establishment of a standardized protocol including the specific enrichment of ADP-ribosylated proteins and peptides and subsequent mass spectrometric analysis allows the identification of ADP-ribose acceptor sites of modified proteins and to address the functional contribution of ADP-ribosylation in vitro as well as in vivo.
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Acknowledgments
The authors would like to thank Dr. Dorothea Rutishauser (former member of the Functional Genomics Center Zurich, University of Zurich, Zurich, Switzerland) for advice and technical assistance. We also thank Felix R. Althaus (Institute of Pharmacology and Toxicology, University of Zurich-Vetsuisse) for providing hPARG expressing baculo virus. Work on ADP-ribosyltransferases in the laboratory of M.O.H is supported by the Swiss National Science Foundation (SNF 31-122421).
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Rosenthal, F., Messner, S., Roschitzki, B., Gehrig, P., Nanni, P., Hottiger, M.O. (2011). Identification of Distinct Amino Acids as ADP-Ribose Acceptor Sites by Mass Spectrometry. In: Tulin, A. (eds) Poly(ADP-ribose) Polymerase. Methods in Molecular Biology, vol 780. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-61779-270-0_4
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DOI: https://doi.org/10.1007/978-1-61779-270-0_4
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