DNMT2 / TRDMT1 Protein

DNA (cytosine-5-)-Methyltransferase 2 / tRNA aspartic acid methyltransferase 1

DNMT2 / TRDMT1 Protein Products

DNMT2 / TRDMT1 Protein, Recombinant

Molecule	Species	Description	Cat. No
DNMT2/TRDMT1	Human	DNMT2/TRDMT1 Protein, Recombinant, With GST Tag	11224-H09B

DNMT2 / TRDMT1 cDNA Clone

Molecule	Species	Description	Cat. No
DNMT2/TRDMT1	Human	Homo sapiens DNMT2/TRDMT1 DNA ORF clone(NM_004412.4)	HG11224-M

DNMT2 / TRDMT1 Related Areas

Enzyme>>Methyltransferase>>DNMT2/TRDMT1

DNMT2 / TRDMT1 Alternative Names

DNMT2, TRDMT1, RP11-406H21.1,  M.HsaIIP, PuMet, RNMT1 [Homo sapiens]

Dnmt2, Trdmt1, RP23-14I24.1, Rnmt2 [Mus musculus]

DNMT2 / TRDMT1 Background

DNMT2, also known as tRNA (cytosine-5-)-methyltransferase, DNA methyltransferase homolog HsaIIP, and TRDMT1, is a member of the DNA methyltransferase family of enzymes. DNMT2 enzymes have been widely conserved during evolution and contain all of the signature motifs of DNA (cytosine-5)-methyltransferases. It contains all 10 sequence motifs that are conserved among m(5)C MTases, including the consensus S:-adenosyl-L-methionine-binding motifs and the active site ProCys dipeptide, and its structure is very similar to prokaryotic DNA methyltransferases. DNMT2 has close homologs in plants, insects and Schizosaccharomyces pombe, but no related sequence can be found in the genomes of Saccharomyces cerevisiae or Caenorhabditis elegans. While the biological function of DNMT2 is not yet known, the strong binding to DNA suggests that DNMT2 may mark specific sequences in the genome by binding to DNA through the specific target-recognizing motif. However, the DNA methyltransferase activity of these proteins is comparatively weak and their biochemical and functional properties remain enigmatic. Recent evidence now shows that Dnmt2 has a novel tRNA methyltransferase activity, raising the possibility that the biological roles of these proteins might be broader than previously thought.

DNMT2 / TRDMT1 Related Studies

1. Dong A, et al. (2001) Structure of human DNMT2, an enigmatic DNA methyltransferase homolog that displays denaturant-resistant binding to DNA. Nucleic Acids Res. 29(2): 439-48.
2. Hermann A, et al. (2003) The human Dnmt2 has residual DNA-(cytosine-C5) methyltransferase activity. J Biol Chem. 278(34): 31717-21.
3. Jeltsch A, et al. (2006) Two substrates are better than one: dual specificities for Dnmt2 methyltransferases. Trends Biochem Sci. 31(6): 306-8.
4. Schaefer M, et al. (2010) Solving the Dnmt2 enigma. Chromosoma. 119(1): 35-40.