Identification of Distinct Amino Acids as ADP-Ribose Acceptor Sites by Mass Spectrometry
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Author / Producer
Date
2011
Publication Type
Book Chapter
ETH Bibliography
yes
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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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Publication status
published
Editor
Book title
Poly(ADP-ribose) Polymerase
Journal / series
Volume
780
Pages / Article No.
57 - 66
Publisher
Humana Press
Event
Edition / version
Methods
Software
Geographic location
Date collected
Date created
Subject
ARTD1; ADP-Ribosylation; Electron transfer dissociation; Boronic acid; Enrichment
Organisational unit
02207 - Functional Genomics Center Zurich / Functional Genomics Center Zurich