期刊
JOURNAL OF PROTEOME RESEARCH
卷 7, 期 3, 页码 1001-1006出版社
AMER CHEMICAL SOC
DOI: 10.1021/pr0705338
关键词
methylation; methylation of aspartic acid; methylation of glutamic acid; mass spectrometry; proteomics
资金
- NCI NIH HHS [CA107943, R33 CA107943, R01 CA126832-01A1, R21 CA107943, R01 CA126832, R21 CA107943-01] Funding Source: Medline
- NCI NIH HHS [R21 CA107943, R33 CA107943, CA107943, R21 CA107943-01] Funding Source: Medline
- NIA NIH HHS [P50AG025688, P50 AG025688] Funding Source: Medline
- NIDDK NIH HHS [R01 DK082664, R01 DK082664-01] Funding Source: Medline
Methylation of lysine and arginine is known to be critical in cellular processes. However, methylation of other amino acidic residues has been largely overlooked. Here, we report a systematic screening for methylation of side chains of aspartate and glutamate (D/E-methylation), involving exhaustive nano-HPLC/MS/MS, a protein sequence database search, and manual verification. The putative D/E-methylated peptides were confirmed by MS/MS of synthetic peptides. Our analysis identified several D/E-methylation substrate proteins and their modification sites in human and yeast cells. To our knowledge, this is the first report conclusively identifying in vivo D/E-methylation substrates and their modification sites in eukaryotic cells, demonstrating that D/E-methylations are abundant protein modifications. The substrate proteins identified here provide a stepping stone for future biochemical characterization of protein methylation pathways.
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