期刊
PROTEIN JOURNAL
卷 28, 期 3-4, 页码 139-147出版社
SPRINGER
DOI: 10.1007/s10930-009-9174-3
关键词
Proteomic analysis; Posttranslational modification; RNA binding proteins; Methylarginine-containing proteins; Protein arginine methylation
资金
- National Science Council of Republic of China [91-3112-B-040-001, 923112-B-040-001, 91-3112-P-001-009-Y]
- Chung Shan Medical University [90-OM-018, 90-OM-090]
- Academia Sinica
Protein arginine methylation is found in many nucleic acid binding proteins affecting numerous cellular functions. In this study we identified methylarginine-containing proteins in HeLa cell extracts by two-dimensional electrophoresis and immunoblotting with a methylarginine-specific antibody. Protein spots with matched protein stain and blotting signals were analyzed by mass spectrometry. The identities of 12 protein spots as 11 different proteins were suggested. Known methylarginine-containing proteins such as hnRNP A2/B1, hnRNP A1, hnRNP G and FUS were identified, indicating the feasibility of our approach. However, four highly abundant metabolic enzymes that might co-electrophorese with methylarginine-containing proteins were also identified. Other nucleic acid binding proteins hnRNP M, hnRNP I and NonO protein were identified. Recombinant hnRNP M and a peptide with the RGG sequence in hnRNP M could be further methylated in vitro. The immunoblotting results of immunoprecipitated hnRNP I and NonO protein are consistent with arginine methylation in both proteins. In this study we identified methylarginine-containing proteins in HeLa cells through proteomic approaches and the method is fast and robust for further applications.
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