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language
eng
Author
Shibata, Tomoko Center for Integrated Research in Science, Shimane University, Faculty of Medicine, Izumo 693-8501, Japan
Yoshino, Ken-ichi
Hara, Nobumasa
Description
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-ADPribosylated 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.
Subject
Arginine-specific ADP-ribosylation
Posttranslational modification
Precursor ion scanning
N-(ADP-ribosyl)-carbodiimide
Ornithine
Mass spectrometry
Journal Title
Analytical Biochemistry
Volume
393
Issue
2
Start Page
248
End Page
254
ISSN
0003-2697
Published Date
2009-10-15
DOI
Publisher
Elsevier
NII Type
Journal Article
Format
PDF
Text Version
著者版
Gyoseki ID
e10622
e10605
OAI-PMH Set
Faculty of Medicine
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