tRNA (uracil (54)-C(5))-methyltransferase (trmA) is an enzymatic protein responsible for methylating the C(5) position of uridine at position 54 (m⁵U54) in bacterial transfer RNA (tRNA). This modification is critical for tRNA stability, codon-anticodon recognition, and translation fidelity . The recombinant form of this enzyme from Pseudomonas syringae pv. tomato (strain DC3000) is commercially available and characterized for structural and functional studies .
trmA catalyzes the methylation of uridine-54 in tRNA, a conserved modification across bacteria. This reaction ensures proper tRNA structure, enhances ribosome binding during translation, and prevents frameshifting or misincorporation of amino acids .
In P. syringae pv. tomato, trmA may contribute to:
Pathogenicity: Efficient protein synthesis during host invasion.
Stress Adaptation: Maintenance of translational accuracy under adverse conditions.
Studies in Pyrococcus abyssi revealed that homologs of trmA (e.g., PAB0719) exhibit TrmA-like activity, methylating uridine-54 in tRNA rather than rRNA. This functional shift highlights evolutionary flexibility in methyltransferase substrate specificity .
Phylogenetic analysis suggests that trmA-like genes in archaea (e.g., Thermococcales) were acquired via horizontal transfer from bacterial donors. This transfer enabled functional adaptation to methylate tRNA instead of rRNA .
The recombinant trmA from P. syringae pv. tomato is used in:
Structural Biology: Crystallization studies to elucidate catalytic mechanisms.
Biochemical Assays: Enzyme activity tests using synthetic tRNA substrates.
Comparative Genomics: Evolutionary studies of tRNA modification systems.
| Feature | trmA (bacterial) | RumA (bacterial) |
|---|---|---|
| Substrate | tRNA (uridine-54) | 23S rRNA (m⁵U1939) |
| SAM dependence | Yes | Yes |
| Functional role | tRNA stability, translation | rRNA maturation, ribosome assembly |
| Example organisms | P. syringae, E. coli | E. coli, P. abyssi |
KEGG: pst:PSPTO_4654
STRING: 223283.PSPTO_4654