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Gene Review

HMT1  -  protein-arginine omega-N methyltransferase...

Saccharomyces cerevisiae S288c

Synonyms: HCP1, Major type I protein arginine N-methyltransferase, ODP1, Protein arginine N-methyltransferase 1, RMT1, ...
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Disease relevance of HMT1

  • Characterization of a novel barley protein, HCP1, that interacts with the Brome mosaic virus coat protein [1].

High impact information on HMT1

  • Furthermore, RNA in situ hybridization analysis demonstrates that loss of Hmt1 results in slowed release of HSP104 mRNA from the sites of transcription [2].
  • Moreover, loss of Hmt1 affects interactions between mRNA-binding proteins and Tho2, a component of the TREX (transcription/export) complex that is important for transcriptional elongation and recruitment of mRNA export factors [2].
  • Hmt1 is the major type I arginine methyltransferase in the yeast Saccharomyces cerevisiae and facilitates the nucleocytoplasmic transport of mRNA-binding proteins through their methylation [2].
  • Hmt1p methylates both Npl3p and Hrp1p, which are shuttling hnRNPs involved in mRNA processing and export [3].
  • Furthermore, we find a genetic relationship between Hmt1p and cap-binding protein 80 (CBP80) [3].

Biological context of HMT1


Anatomical context of HMT1


Associations of HMT1 with chemical compounds

  • We first developed an in vivo assay to identify proteins methylated by the Hmt1 arginine methyltransferase [10].
  • Following SDS polyacrylamide electrophoresis, 11 distinct proteins were identified as substrates for the Hmt1 methyltransferase [10].
  • Vacuolar uptake of Cd2+ and of a glutathione conjugate were also observed, but are not attributable to HMT1 [8].
  • Intact yeast cells lacking RMT1, the gene encoding the protein omega-NG-arginine methyltransferase, were labeled with the methyl donor S-adenosyl-L-[methyl-3H]methionine [11].
  • Npl3 with all 15 RGG arginines mutated to lysine exited the nucleus independent of Hmt1, indicating a direct effect of methylation on Npl3 transport [12].

Physical interactions of HMT1

  • However, cells missing HMT1 and also bearing mutations in the mRNA-binding proteins Npl3p or Cbp80p can no longer survive, providing genetic backgrounds in which to study Hmt1p function [5].
  • Air2p also has a RING finger domain and was bound to Hmt1p [13].

Regulatory relationships of HMT1


Other interactions of HMT1

  • We demonstrate that Npl3p is methylated by Hmt1p both in vivo and in vitro [4].
  • The observation that three nucleolar proteins are modified by Hmt1p but are not exported from the nucleolus implies an alternate role for arginine methylation [10].
  • Genome-wide location analysis shows that Hmt1 is bound to specific functional gene classes, many of which are also bound by Tho2 and other mRNA-processing factors [2].
  • Furthermore, we show that Nab2p is modified within its RGG domain by the type I protein-arginine methyltransferase, Hmt1p [14].
  • We found that we could distinguish PRMT family members by their sensitivity to these reagents; JBP1/PRMT5 and Hsl7 methyltransferases were inhibited in a similar manner as PRMT3, whereas Rmt1, PRMT1, and CARM1/PRMT4 were not affected [15].

Analytical, diagnostic and therapeutic context of HMT1

  • Northern blot analysis revealed that multicopies of the yeast and human HCP1, as well as TGFR, resulted in an increase in the IN01 mRNA level in the yeast mutant [16].
  • HCP1 was found predominantly in the soluble fractions after differential centrifugation of BMV-infected and mock-inoculated barley tissues [1].


  1. Characterization of a novel barley protein, HCP1, that interacts with the Brome mosaic virus coat protein. Okinaka, Y., Mise, K., Okuno, T., Furusawa, I. Mol. Plant Microbe Interact. (2003) [Pubmed]
  2. Arginine methyltransferase affects interactions and recruitment of mRNA processing and export factors. Yu, M.C., Bachand, F., McBride, A.E., Komili, S., Casolari, J.M., Silver, P.A. Genes Dev. (2004) [Pubmed]
  3. Arginine methylation facilitates the nuclear export of hnRNP proteins. Shen, E.C., Henry, M.F., Weiss, V.H., Valentini, S.R., Silver, P.A., Lee, M.S. Genes Dev. (1998) [Pubmed]
  4. A novel methyltransferase (Hmt1p) modifies poly(A)+-RNA-binding proteins. Henry, M.F., Silver, P.A. Mol. Cell. Biol. (1996) [Pubmed]
  5. Analysis of the yeast arginine methyltransferase Hmt1p/Rmt1p and its in vivo function. Cofactor binding and substrate interactions. McBride, A.E., Weiss, V.H., Kim, H.K., Hogle, J.M., Silver, P.A. J. Biol. Chem. (2000) [Pubmed]
  6. Disruptor of telomeric silencing-1 is a chromatin-specific histone H3 methyltransferase. Lacoste, N., Utley, R.T., Hunter, J.M., Poirier, G.G., Côte, J. J. Biol. Chem. (2002) [Pubmed]
  7. Design of allele-specific protein methyltransferase inhibitors. Lin, Q., Jiang, F., Schultz, P.G., Gray, N.S. J. Am. Chem. Soc. (2001) [Pubmed]
  8. Transport of metal-binding peptides by HMT1, a fission yeast ABC-type vacuolar membrane protein. Ortiz, D.F., Ruscitti, T., McCue, K.F., Ow, D.W. J. Biol. Chem. (1995) [Pubmed]
  9. apd1+, a gene required for red pigment formation in ade6 mutants of Schizosaccharomyces pombe, encodes an enzyme required for glutathione biosynthesis: a role for glutathione and a glutathione-conjugate pump. Chaudhuri, B., Ingavale, S., Bachhawat, A.K. Genetics (1997) [Pubmed]
  10. In vivo analysis of nucleolar proteins modified by the yeast arginine methyltransferase Hmt1/Rmt1p. Xu, C., Henry, P.A., Setya, A., Henry, M.F. RNA (2003) [Pubmed]
  11. delta-N-methylarginine is a novel posttranslational modification of arginine residues in yeast proteins. Zobel-Thropp, P., Gary, J.D., Clarke, S. J. Biol. Chem. (1998) [Pubmed]
  12. Arginine methylation of yeast mRNA-binding protein Npl3 directly affects its function, nuclear export, and intranuclear protein interactions. McBride, A.E., Cook, J.T., Stemmler, E.A., Rutledge, K.L., McGrath, K.A., Rubens, J.A. J. Biol. Chem. (2005) [Pubmed]
  13. Novel RING finger proteins, Air1p and Air2p, interact with Hmt1p and inhibit the arginine methylation of Npl3p. Inoue, K., Mizuno, T., Wada, K., Hagiwara, M. J. Biol. Chem. (2000) [Pubmed]
  14. Nab2p is required for poly(A) RNA export in Saccharomyces cerevisiae and is regulated by arginine methylation via Hmt1p. Green, D.M., Marfatia, K.A., Crafton, E.B., Zhang, X., Cheng, X., Corbett, A.H. J. Biol. Chem. (2002) [Pubmed]
  15. PRMT3 is a distinct member of the protein arginine N-methyltransferase family. Conferral of substrate specificity by a zinc-finger domain. Frankel, A., Clarke, S. J. Biol. Chem. (2000) [Pubmed]
  16. Structural and functional conservation of human and yeast HCP1 genes which can suppress the growth defect of the Saccharomyces cerevisiae ire15 mutant. Nikawa, J., Nakano, H., Ohi, N. Gene (1996) [Pubmed]
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