Regulation of post-translational protein arginine methylation during HeLa cell cycle
- Authors
- Kim, Chongtae; Lim, Yongchul; Yoo, Byong Chul; Won, Nam Hee; Kim, Sangduk; Kim, Gieun
- Issue Date
- 9월-2010
- Publisher
- ELSEVIER SCIENCE BV
- Keywords
- omega-N-G,N-G-asymmetric and omega-N-G,N ' (G)-symmetric dimethyl-arginine; Hela cell cycle; Protein arginine methyltransferases; Heterogeneous nuclear ribonucleoprotein R; Cleavage stimulation factor 64 kDa subunit; Triosephosphate isomerase
- Citation
- BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, v.1800, no.9, pp.977 - 985
- Indexed
- SCIE
SCOPUS
- Journal Title
- BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
- Volume
- 1800
- Number
- 9
- Start Page
- 977
- End Page
- 985
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/115825
- DOI
- 10.1016/j.bbagen.2010.06.004
- ISSN
- 0304-4165
- Abstract
- Background: Post-translational arginine methylation which modifies protein-arginyl residues by protein arginine methyltransferase (PRMT) was investigated during synchronized HeLa cell cycle. Methods: The lysates of cells synchronized at each stage were subjected to one and/or two dimensional electrophoresis followed by Western immunoblot using against anti-asymmetric-dimethyl-arginine (ASYM24), anti-symmetric-dimethyl-arginine (SYM10), and subclasses of PRMTs, including PRMT1, PRMT3, PRMT4 (CARM1), PRMT5, PRMT6, and PRMT7 antibodies. Results: Proteins with approximate molecular masses of 80 kDa, 68 kDa, and 64 kDa, containing asymmetric-dimethyl-arginine (aDMA) were increased at G0/G1 to G1, which lasted until S phase. In addition. 25 kDa protein of symmetric-dimethyl-arginine (sDMA) was also markedly up-regulated from G0/G1 to G1. The levels of PRMT3, PRMT6 and PRMT7 were concurrently increased during the cell cycle. Two-dimensional gel electrophoresis followed by MALDI-TOF-MS was identified as aDMA-80 kDa and aDMA-68 kDa proteins as heterogeneous nuclear ribonucleoprotein R (hnRNPR), aDMA-64 kDa proteins as cleavage stimulation factor 64 kDa subunit (CstF-64), and sDMA-25 kDa protein as triosephosphate isomerase (TPI). The levels of increased aDMA of hnRNPR were reduced, when HeLa cells were transfected with siRNA for PRMT1, and the aDMA of CstF-64 with siRNA for PRMT3, while depletion of PRMT5 down-regulated sDMA of TPI. Conclusion: Protein arginine dimethylations of hnRNPR, CstF-64, and TPI were regulated during HeLa cell cycle by respective PRMTs. General significance: These results suggest that regulation of arginine dimethylation of hnRNPR, CstF-64, and TPI at G0/G1 to G1 are most likely to modulate the cellular growth and proliferation in HeLa cell cycle. (C) 2010 Elsevier B.V. All rights reserved.
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