Identification of protein O-GlcNAcylation sites using electron transfer dissociation mass spectrometry on native peptides.

ABSTRACT: Protein O-GlcNAcylation occurs in all animals and plants and is implicated in modulation of a wide range of cytosolic and nuclear protein functions, including gene silencing, nutrient and stress sensing, phosphorylation signaling, and diseases such as diabetes and Alzheimer's. The limiting factor impeding rapid progress in deciphering the biological functions of protein O-GlcNAcylation has been the inability to easily identify exact residues of modification. We describe a robust, high-sensitivity strategy able to assign O-GlcNAcylation sites of native modified peptides using electron transfer dissociation mass spectrometry. We have studied the murine postsynaptic density pseudoorganelle and report the assignment of 58 modification sites from a single experiment--significantly increasing th

SUBMITTER: Chalkley RJ 

PROVIDER: S-EPMC2690010 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature