Proteomic analysis of stable protein methylation in lymphoblastoid cells.
We investigated the global distribution of methylaccepting proteins in lymphoblastoid cells by two-dimensional (2-D) gel electrophoresis. The 2-D electrophoreograms of normal and hypo-methylation (cells grown with a methyltransferase inhibitor adenosine dialdehyde) protein extracts did not exhibit significant differences. However, in vitro methylation of the hypomethylated extracts in the presence of the methyl-group donor S-adenosyl-[methyl-3H]-methionine revealed close to a hundred signals. Less than one-fifth of the signals could be correlated with protein stains, indicating that most of the methylaccepting proteins are low abundant ones. We analyzed six of the spots that can be correlated with protein stains and suggested their identities. Among these putative protein methylacceptors, three are heterogeneous nuclear ribonucleoproteins (hnRNPA2/B1 and hnRNP K) that are reportedly methylated in their arginine- and glycine-rich RGG motifs.
Huang
Hung-Ming
HM
Institute of Medicine, Chung Shan Medical and Dental University, Sec. Chien-Kuo N. Rd, Taichung, Taiwan, ROC.
Tam
Ming F
MF
Tam
Tsuey-Chyi S
TC
Chen
Da-Huang
DH
Hsieh
Mingli
M
Li
Chuan
C
D015180:Electrophoresis, Gel, Two-Dimensional; D007945:Leukemia, Lymphoid / Q000378:metabolism*; D008214:Lymphocytes / Q000737:chemistry / Q000378:metabolism*; D008745:Methylation; D011506:Proteins / Q000737:chemistry*; D020543:Proteome
D011506:Proteins; D020543:Proteome