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Submitted on March 19, 2003
Dept. of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, CA 94143
Corresponding Author: robertc{at}itsa.ucsf.edu
The addition of a single N-acetylglucosamine moiety O-linked to serine and threonine residues of nuclear and cytoplasmic proteins is a widespread post-translational modification. The conventional method for detecting and locating sites of modification is through a multi-step radioactivity-based approach. We have recently shown that sites of O-GlcNAc modification can be determined using Q-TOF tandem mass spectrometry [Chalkley, R. J. and Burlingame, A. L., (2001). J. Am. Soc. Mass Spec. 12, 1106-1113]. In this work utilization of this new approach has revealed previously undetected sites of O-GlcNAc modification of the transcription factor Serum Response Factor (SRF).
Revised on April 8, 2003
Accepted on April 8, 2003
Identification of novel sites of O-GlcNAc modification of serum response factor using Q-TOF mass spectrometry
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