Strategy for comprehensive identification of post-translational modifications in cellular proteins, including low abundant modifications: application to glyceraldehyde-3-phosphate dehydrogenase

Journal of Proteome Research
Jawon SeoKong-Joo Lee

Abstract

Post-translational modifications (PTMs) play key roles in the regulation of biological functions of proteins. Although some progress has been made in identifying several PTMs using existing approaches involving a combination of affinity-based enrichment and mass spectrometric analysis, comprehensive identification of PTMs remains a challenging problem in proteomics because of the dynamic complexities of PTMs in vivo and their low abundance. We describe here a strategy for rapid, efficient, and comprehensive identification of PTMs occurring in biological processes in vivo. It involves a selectively excluded mass screening analysis (SEMSA) of unmodified peptides during liquid chromatography-electrospray ionization-quadrupole-time-of-flight tandem mass spectrometry (LC-ESI-q-TOF MS/MS) through replicated runs of a purified protein on two-dimensional gel. A precursor ion list of unmodified peptides with high mass intensities was obtained during the initial run followed by exclusion of these unmodified peptides in subsequent runs. The exclusion list can grow as long as replicate runs are iteratively performed. This enables the identifications of modified peptides with precursor ions of low intensities by MS/MS sequencing. Applicatio...Continue Reading

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Citations

Oct 18, 2008·Bioconjugate Chemistry·Giselle M KnudsenV Jo Davisson
Aug 9, 2008·Journal of Proteome Research·Christian BaumgartnerBarry L Karger
Dec 15, 2010·Molecular & Cellular Proteomics : MCP·Jaeho JeongKong-Joo Lee
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Oct 30, 2014·ACS Chemical Biology·Jae-Jin LeeKong-Joo Lee
Aug 29, 2014·Journal of Proteome Research·Zuo-Fei YuanBenjamin A Garcia
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Jan 21, 2015·Biochemical and Biophysical Research Communications·Moon-Jung KimHwa-Young Kim
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