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PRMT3  -  protein arginine methyltransferase 3

Homo sapiens

Synonyms: HRMT1L3, Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3, Protein arginine N-methyltransferase 3
 
 
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Disease relevance of PRMT3

 

High impact information on PRMT3

 

Biological context of PRMT3

  • In vitro binding assays demonstrated that this was an interaction occurring via the C-terminal catalytic core domain of PRMT3 [4].
  • PRMT3 is unique in that its N-terminus harbours a C2H2 zinc-finger domain that is proposed to confer substrate specificity [5].
  • With GST-PRMT3, however, only nine dimethylated arginines, located mainly in the C-terminal region of EWS protein, could be assigned, indicating that structural determinants prevent complete methylation [6].
 

Associations of PRMT3 with chemical compounds

  • Using purified recombinant protein arginine methyltransferases (PRMTs), we showed that the C-terminal domain could be methylated by PRMT1, PRMT3, and PRMT4 in vitro and that both the R(544)-K mutant and the R(546)-K mutant were refractory toward these enzymes [7].
 

Other interactions of PRMT3

 

Analytical, diagnostic and therapeutic context of PRMT3

References

  1. Unusual sites of arginine methylation in Poly(A)-binding protein II and in vitro methylation by protein arginine methyltransferases PRMT1 and PRMT3. Smith, J.J., Rücknagel, K.P., Schierhorn, A., Tang, J., Nemeth, A., Linder, M., Herschman, H.R., Wahle, E. J. Biol. Chem. (1999) [Pubmed]
  2. PRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunits. Bachand, F., Silver, P.A. EMBO J. (2004) [Pubmed]
  3. PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation. Tang, J., Gary, J.D., Clarke, S., Herschman, H.R. J. Biol. Chem. (1998) [Pubmed]
  4. DAL-1/4.1B tumor suppressor interacts with protein arginine N-methyltransferase 3 (PRMT3) and inhibits its ability to methylate substrates in vitro and in vivo. Singh, V., Miranda, T.B., Jiang, W., Frankel, A., Roemer, M.E., Robb, V.A., Gutmann, D.H., Herschman, H.R., Clarke, S., Newsham, I.F. Oncogene (2004) [Pubmed]
  5. Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3). Swiercz, R., Person, M.D., Bedford, M.T. Biochem. J. (2005) [Pubmed]
  6. Different methylation characteristics of protein arginine methyltransferase 1 and 3 toward the Ewing Sarcoma protein and a peptide. Pahlich, S., Bschir, K., Chiavi, C., Belyanskaya, L., Gehring, H. Proteins (2005) [Pubmed]
  7. Alternative splicing modulates protein arginine methyltransferase-dependent methylation of fragile X syndrome mental retardation protein. Dolzhanskaya, N., Merz, G., Denman, R.B. Biochemistry (2006) [Pubmed]
  8. Effects of ADMA upon gene expression: an insight into the pathophysiological significance of raised plasma ADMA. Smith, C.L., Anthony, S., Hubank, M., Leiper, J.M., Vallance, P. PLoS Med. (2005) [Pubmed]
 
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