title: Regulation of post-translational protein arginine methylation during HeLa cell cycle.
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.
  
  
  CONCLUSIONS
  Protein arginine dimethylations of hnRNPR, CstF-64, and TPI were regulated during HeLa cell cycle by respective PRMTs.
  
  
  CONCLUSIONS
  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.
authors.affiliation: Department of Biological Engineering, Graduate School of Seokyeong University, Seoul 136-704, Republic of Korea.
authors.forename: Chongtae
authors.initials: C
authors.lastname: Kim
authors.forename: Yongchul
authors.initials: Y
authors.lastname: Lim
authors.forename: Byong Chul
authors.initials: BC
authors.lastname: Yoo
authors.forename: Nam Hee
authors.initials: NH
authors.lastname: Won
authors.forename: Sangduk
authors.initials: S
authors.lastname: Kim
authors.forename: Gieun
authors.initials: G
authors.lastname: Kim
mesh_terms: D001120:Arginine / Q000378:metabolism; D039241:Cleavage Stimulation Factor; D016193:G1 Phase / Q000502:physiology*; D006367:HeLa Cells; D034441:Heterogeneous-Nuclear Ribonucleoproteins / Q000378:metabolism*; D006801:Humans; D008745:Methylation; D011499:Protein Processing, Post-Translational / Q000502:physiology*; D011484:Protein-Arginine N-Methyltransferases / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000378:metabolism*; D016192:Resting Phase, Cell Cycle / Q000502:physiology*; D014305:Triose-Phosphate Isomerase / Q000378:metabolism*
chemical_list: C474466:CSTF2T protein, human; D039241:Cleavage Stimulation Factor; D034441:Heterogeneous-Nuclear Ribonucleoproteins; D016601:RNA-Binding Proteins; D001120:Arginine; D011484:Protein-Arginine N-Methyltransferases; D014305:Triose-Phosphate Isomerase