EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
  2.1.1.215 | 4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNA |
- |
Pyrococcus furiosus |
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNA |
- |
? |
| 2.1.1.215 | 4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNA |
- |
Aquifex aeolicus |
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNA |
- |
? |
| 2.1.1.215 | 4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNA |
the T-arm in tRNA is the binding site of Trm1, multisite specificity, tRNA-docking modeling, overview |
Aquifex aeolicus |
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNA |
- |
? |
| 2.1.1.215 | 4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNACys |
m2G26 formation is faster than the m2G27 formation and disruption of the G27-C43 base pair accelerates velocity of the G27 modification. A fraction of native tRNACys has a N2-dimethylguanine26/N2-dimethylguanine27 modification. Initially the N2-methylguanine26 modification occurs, and then the second methyl transfer reaction generates N2-dimethylguanine26. The third methyl transfer reaction modifies guanine 27 to N2-methylguanine27 followed by a fourth methylation of N2-methylguanine27 to N2-dimethylguanine27 |
Aquifex aeolicus |
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNACys |
- |
? |
| 2.1.1.215 | 4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNAPhe |
tRNAPhe from yeast |
Pyrococcus furiosus |
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNAPhe |
- |
? |
| 2.1.1.215 | 4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNAPhe |
tRNAPhe from yeast |
Aquifex aeolicus |
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNAPhe |
- |
? |
| 2.1.1.215 | more |
Aquifex aeolicus TRm1 may recognize only D-stem structure and guanine26 residue |
Aquifex aeolicus |
? |
- |
? |
| 2.1.1.215 | more |
recognition mechanisms of the Trm1 proteins: Aquifex aeolicus Trm1 recognizes the guanine26 and guanine27 bases from the T-arm. In contrast, archaeal and eukaryotic Trm1 proteins recognize the guanine26 base from the D-stem and variable region. The distance between the T-arm and guanine26 (or guanine27) is longer than the distance between the D-stem, variable region, and guanine26. These differences from binding site to the target guanine base(s) may decide the multisite or single site recognition of the Trm1 proteins |
Aquifex aeolicus |
? |
- |
? |
| 2.1.1.215 | more |
yeast tRNAPhe and Escherichia coli tRNALeu transcripts are methylated. In contrast, Escherichia coli tRNASer is not methylated, because this tRNA possesses adenine26 sequence instead of guanine26 |
Aquifex aeolicus |
? |
- |
? |
| 2.1.1.215 | more |
Trm1 catalyzes methyl transfers to class II tRNAs as well as all class I tRNAs, the size and sequence of the variable region are not recognized by Aquifex aeolicus Trm1, all tRNA transcripts are methylated. tRNA recognition mechanism of multisite specific Trm1, Asp132 is a catalytic center, structure-function analysis, overview |
Aquifex aeolicus |
? |
- |
? |
