A recent biochemical study has demonstrated that the 3′ terminal nucleotide of Turnip Yellow Mosaic Virus (TYMV) RNA—identified within the 23-25 S region—can be specifically esterified with the amino acid valine. This process occurs in the presence of adenosine triphosphate (ATP) and an enzyme preparation derived from the bacterium Escherichia coli.
The research suggests that viral RNA possesses structural features that allow it to mimic the function of transfer RNA (tRNA), which is typically responsible for the aminoacylation process during protein synthesis. This phenomenon, known as tRNA mimicry, is observed here as TYMV RNA appears to be recognized by a tRNA synthetase-like enzyme from E. coli, thereby permitting the attachment of an amino acid to its terminal nucleotide.
Furthermore, analysis of the sequence around the valine-binding site on TYMV RNA revealed a nucleotide composition distinct from that of authentic tRNA(Val) extracted from cabbage, indicating that while the viral RNA can functionally imitate tRNA in binding valine, its sequence and structure remain unique.
The findings contribute to the broader understanding of viral molecular biology, offering insights into how plant viruses may exploit host cellular machinery for replication or protein translation. More importantly, it opens new avenues for exploring how viruses can hijack host enzymes and pathways through molecular mimicry.
Future research may explore the extent to which such aminoacylation influences TYMV’s replication cycle or pathogenicity, and whether this mechanism is common among other plant viruses.
Source: https:// – Courtesy of the original publisher.
