Wang Q(1)(2), Li Z(1)(3), Zhou J(1)(2), Wang Y(1)(2), Wang K(1)(2), Qin H(1)(2), Ye M(1)(2). Author information:
(1)CAS Key Laboratory of Separation Sciences for Analytical Chemistry, National
Chromatographic R&A Center, Dalian Institute of Chemical Physics, Chinese
Academy of Sciences, Dalian 116023, China.
(2)University of Chinese Academy of Sciences, Beijing 100049, China.
(3)Shanghai Key Laboratory of Functional Materials Chemistry, Department of
Chemistry and Molecular Engineering, East China University of Science and
Technology, Shanghai 200237, China.
Protein methylation, especially that occurs on arginine and lysine residues, is one of the most important post-translational modifications involved in various cellular processes including RNA splicing, DNA repair, and so forth. Systematic analysis of protein methylation would facilitate the understanding of its regulatory mechanisms. Strong cation chromatography has been used to globally analyze arginine/lysine methylation at the proteome scale with good performance. However, the co-enriched histidine-containing peptides severely interfere with the detection of low-abundance methylpeptides. Here, we developed a novel chemical strategy which enabled almost complete depletion of histidine-containing peptides in the protein digest, thereby resulting in the identification of more low-abundance arginine/lysine methylpeptides. Totally, 333 arginine and lysine methylation forms from 207 proteins were identified in this study. Overall, the number of methylation identifications increased about 50% by using our new method. Data are available via ProteomeXchange with the identifier PXD023845.
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