Journal
ANALYTICAL BIOCHEMISTRY
Volume 393, Issue 2, Pages 248-254Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ab.2009.06.028
Keywords
Arginine-specific ADP-ribosylation; Posttranslational modification; Precursor ion scanning; N-(ADP-ribosyl)-carbodiimide; Ornithine; Mass spectrometry
Funding
- Japan Society for the Promotion of Science [18924005]
- Grants-in-Aid for Scientific Research [18924005] Funding Source: KAKEN
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Arginine (Arg)-specific ADP-ribosylation is one of the posttranslational modifications of proteins and is thought to play an important role in reversibly regulating functions of the target proteins in eukaryotes. However, the physiological target protein has not been established. We examined the fragmentation pattern of both ADP-ribosyl-Arg (ADP-R-Arg) and Arg-ADP-ribosylated peptides by quadrupole tandem mass spectrometry and found a specific cleavage of ADP-R-Arg into N-(ADP-ribosyl)-carbodiimide (ADP-R-carbodiimide) and ornithine. Based on this specific fragmentation pattern, we successfully identified the modification site and sequence of Arg-ADP-ribosylated peptide using a two-step collision and showed that ADP-R-carbodiimide is an excellent marker ion for precursor ion scanning of Arg-ADP-ribosylated peptide. We propose that a combination of the precursor ion scanning with ADP-R-carbodiimide as a marker ion and two-step collision is useful in searching for physiological target proteins of Arg-ADP-ribosylation. (C) 2009 Elsevier Inc. All rights reserved.
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