EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   2.1.1.202 | more |
the enzyme Trm4 fabricate 5-methylcytosine (m5C) in RNA molecules utilizing a dual-cysteine catalytic mechanism |
Saccharomyces cerevisiae |
? |
- |
? |
| 2.1.1.202 | more |
the iCLIP method identifies tRNA AspGTC, ValAAC, GlyGCC, and LeuCAA as methylation substrates with methylation within the variable arm at cytosines 48, 49, and 50, no additional NSun2 target sites outside the variable arm. vtRNAs are methylation substrates for NSun2, vtRNAs are ncRNAs found as part of the vault ribonucleoprotein complex |
Homo sapiens |
? |
- |
? |
| 2.1.1.202 | more |
development and evaluation of 5-azacytidine-mediated RNA immunoprecipitation, a mechanism-based technique in nine steps that exploits the covalent bond formed between an RNA methyltransferase and the cytidine analogue 5-azacytidine to recover RNA targets by immunoprecipitation, overview. The method enables over 200fold enrichment of tRNAs that are known targets of the enzyme revealing many tRNA and non-coding RNA targets not previously associated with NSUN2. High frequency of C>G transversions at the cytosine residues targeted by the enzyme, allowing identification of the specific methylated cytosine(s) in target RNAs. tRNAGly(GCC), bears four NSUN2 target sites (C40, 48, 49 and 50) |
Homo sapiens |
? |
- |
? |
| 2.1.1.202 | more |
development and evaluation of a customized version of the individual-nucleotide-resolution crosslinking and immunoprecipitation (iCLIP) method for detection of cytosine methylation in RNA species, site-specific methylation in tRNAs and additional messenger and noncoding RNAs (ncRNAs), overview. Identified NSun2 targets are tRNAs, mRNAs, and ncRNAs |
Homo sapiens |
? |
- |
? |
| 2.1.1.202 | more |
motif I is essential for methyltransferase activity and is required for S-adenosyl-L-methionine binding and catalysis. Enzyme variant Trm4a is lacking motif I in contrast to enzyme variant Trm4b |
Arabidopsis thaliana |
? |
- |
? |
| 2.1.1.202 | more |
the enzyme forms covalent complexes with previously methylated RNA requiring S-adenosyl-L-homocysteine, the removal of this metabolite results in the disassembly of preexisting complexes |
Saccharomyces cerevisiae |
? |
- |
? |
| 2.1.1.202 | more |
C34 methylation depends on Trm4a in both tRNALeuCAA and tRNAProCGG. Substrate specificity, comparison to trm4b, overview |
Schizosaccharomyces pombe |
? |
- |
- |
| 2.1.1.202 | more |
susbtrate specificity of NSUN2, overview. NSUN2 has a much broader target spectrum and is able to modify several positions (C34, C40, C48, C49, and C50) in a number of different tRNAs, as well as other RNA substrates. The enzyme is also active with various mRNAs. M5C modifications in cytoplasmic and mitochondrial tRNAs. Three-dimensional L-shape structure of a tRNA with the positions of m5C modifications and the cognate methyltransferases responsible for installing them marked. The m5C modifications in cytoplasmic and mitochondrial tRNAs. Schematic secondary structure and three-dimensional L-shape structure of a tRNA with the positions of m5C modifications. The broad-spectrum methyltransferase NSUN2 has been suggested to recognize different features in its diverse substrate RNAs. The reported NSUN2-mediated m5C modifications in mRNAs typically lie within highly GC-rich regions, suggesting that the enzyme may preferentially bind such sequences. But all the known NSUN2-mediated m5C modifications in vtRNAs lie within a UCG motif, and mutagenic analysis of the NSUN2 target pre-tRNALeu reveals a consensus sequence of C/A/U32-U/A33-m5C34-A35-A36-G37 |
Homo sapiens |
? |
- |
- |
| 2.1.1.202 | more |
susbtrate specificity of NSUN6, overview |
Pyrococcus horikoshii |
? |
- |
- |
| 2.1.1.202 | more |
susbtrate specificity of NSUN6, overview. Three-dimensional L-shape structure of a tRNA with the positions of m5C modifications and the cognate methyltransferases responsible for installing them marked. The m5C modifications in cytoplasmic and mitochondrial tRNAs. Schematic secondary structure and three-dimensional L-shape structure of a tRNA with the positions of m5C modifications, determination of the interaction sites of NSUN6 with the discriminator base and additional base pairs in the acceptor stem and the D-loop, as observed by X-ray crystallography, overview. m5C72 modifications installed by NSUN6 lie within the acceptor stem of tRNA. NSUN6 forms extensive contacts with its substrate tRNAs. Binding of NSUN6 disrupts base pairing within the tRNA acceptor stem and promotes base-flipping of C71 to make the C5 atom of the C72 nucleotide, which is normally base paired with G1, accessible for methylation. NSUN6 also has a PUA domain that binds to the D-stem region of substrate tRNAs, as well as the non-genomically encoded CCA 3' end. Consistent with this binding mode, the presence of the CCA is found to be an essential pre-requisite for methylation of tRNACys and tRNAThr by NUSN6 |
Homo sapiens |
? |
- |
- |
