Document Detail


Electron transfer dissociation (ETD): the mass spectrometric breakthrough essential for O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1.
MedLine Citation:
PMID:  23335398     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The development of electron-based, unimolecular dissociation MS, i.e. electron capture and electron transfer dissociation (ECD and ETD, respectively), has greatly increased the speed and reliability of labile PTM site assignment. The field of intracellular O-GlcNAc (O-linked N-acetylglucosamine) signaling has especially advanced with the advent of ETD MS. Only within the last five years have proteomic-scale experiments utilizing ETD allowed the assignment of hundreds of O-GlcNAc sites within cells and subcellular structures. Our ability to identify and unambiguously assign the site of O-GlcNAc modifications using ETD is rapidly increasing our understanding of this regulatory glycosylation and its potential interaction with other PTMs. Here, we discuss the advantages of using ETD, complimented with collisional-activation MS, in a study of the extensively O-GlcNAcylated protein Host Cell Factor C1 (HCF-1). HCF-1 is a transcriptional coregulator that forms a stable complex with O-GlcNAc transferase and controls cell cycle progression. ETD, along with higher energy collisional dissociation (HCD) MS, was employed to assign the PTMs of the HCF-1 protein isolated from HEK293T cells. These include 19 sites of O-GlcNAcylation, two sites of phosphorylation, and two sites bearing dimethylarginine, and showcase the residue-specific, PTM complexity of this regulator of cell proliferation.
Authors:
Samuel A Myers; Salima Daou; El Bachir Affar; Al Burlingame
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Proteomics     Volume:  13     ISSN:  1615-9861     ISO Abbreviation:  Proteomics     Publication Date:  2013 Mar 
Date Detail:
Created Date:  2013-03-13     Completed Date:  2013-08-29     Revised Date:  2013-12-09    
Medline Journal Info:
Nlm Unique ID:  101092707     Medline TA:  Proteomics     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  982-91     Citation Subset:  IM    
Copyright Information:
© 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Chromatography, High Pressure Liquid
Glycopeptides / chemistry,  isolation & purification
Glycosylation
HEK293 Cells
Host Cell Factor C1 / chemistry*,  isolation & purification,  metabolism
Humans
Mice
Molecular Sequence Data
Peptide Fragments / chemistry,  isolation & purification
Protein Processing, Post-Translational*
Spectrometry, Mass, Electrospray Ionization / methods
Tandem Mass Spectrometry / methods
Grant Support
ID/Acronym/Agency:
8P41GM103481/GM/NIGMS NIH HHS; MOP115132//Canadian Institutes of Health Research; P41 GM103481/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Glycopeptides; 0/HCFC1 protein, human; 0/Host Cell Factor C1; 0/Peptide Fragments

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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