Issue 11, 2022

Quantitative profiling of PTM stoichiometry by resolvable mass tags

Abstract

Post-translational modifications (PTMs) play important roles in modulating the biological functions of proteins. Stoichiometry, which quantifies the modification percentage, is a critical factor for any given PTM. In this work, we developed a chemoproteomic strategy called “STO-MS” to systematically quantify the PTM stoichiometry in complex biological samples. This strategy employs a resolvable mass tag to differentiate proteoforms with different numbers of modifications and utilizes liquid chromatography coupled with tandem mass spectrometry (LC-MS/MS) techniques to measure PTM stoichiometry at the proteomic level. As a proof-of-concept, we successfully determined the stoichiometry of 197 proteins modified by 4-hydroxynonenal (HNE), a well-characterized lipid-derived electrophile and biomarker for oxidative stress. Our work expands the toolbox for quantification of PTM stoichiometry and sheds light on understanding the biological significance of PTMs in oxidative stress.

Graphical abstract: Quantitative profiling of PTM stoichiometry by resolvable mass tags

Supplementary files

Article information

Article type
Communication
Submitted
05 Aug 2022
Accepted
21 Sep 2022
First published
05 Oct 2022
This article is Open Access
Creative Commons BY-NC license

RSC Chem. Biol., 2022,3, 1320-1324

Quantitative profiling of PTM stoichiometry by resolvable mass tags

Y. Chen, B. Quan, Y. Li, Y. Liu, W. Qin and C. Wang, RSC Chem. Biol., 2022, 3, 1320 DOI: 10.1039/D2CB00179A

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