文献类型：期刊文献

英文题名：Chemical Depletion of Histidine-Containing Peptides Allows Identification of More Low-Abundance Methylation Sites from Proteome Samples

作者：Wang, Qi[1,2];Li, Zhouxian[1,3];Zhou, Jiahua[1,2];Wang, Yan[1,2];Wang, Keyun[1,2];Qin, Hongqiang[1,2];Ye, Mingliang[1,2]

机构：[1]Chinese Acad Sci, Natl Chromatog R&A Ctr, Dalian Inst Chem Phys, CAS Key Lab Separat Sci Analyt Chem, Dalian 116023, Peoples R China;[2]Univ Chinese Acad Sci, Beijing 100049, Peoples R China;[3]East China Univ Sci & Technol, Dept Chem & Mol Engn, Shanghai Key Lab Funct Mat Chem, Shanghai 200237, Peoples R China

年份：2021

卷号：20

期号：5

起止页码：2497

外文期刊名：JOURNAL OF PROTEOME RESEARCH

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000649269600030)】；

基金：This work was supported, in part, by funds from the National Key Research and Development Program of China (2016YFA0501402, 2017YFA0505003, and 2020YFE0202200), the National Natural Science Foundation of China (91753105), the LiaoNing Revitalization Talents Program, and the innovation program of science and research from the DICP, CAS (DICP I201935 and DICP&QIBEBT UN201802) and supported by the Innovation Academy for Precision Measurement Science and Technology, CAS.

语种：英文

外文关键词：methylproteome; depletion of histidine-containing peptides; arginine methylation; lysine methylation; antibody-free

摘要：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.