Bacterial ribonuclease P (RNase P)

Bacterial ribonuclease P (RNase P) is an essential ribonucleoprotein enzyme found in all bacteria, where it catalyzes the site-specific cleavage of the 5'-leader sequence from precursor transfer RNA (tRNA) molecules (Altman, 2007). This maturation step is critical for the translation machinery and overall protein synthesis. The bacterial holoenzyme is typically composed of a single catalytic RNA (P RNA) and a single small protein (P protein), a simpler architecture compared to the multi-protein eukaryotic versions (Gopalan et al., 2018). Due to its essentiality and the structural divergence between bacterial and human RNase P, it is considered a high-priority target for the development of new classes of antibiotics. Inhibiting RNase P leads to the accumulation of non-functional tRNA precursors, effectively arresting bacterial metabolism and growth. Therapeutic strategies include small molecule inhibitors, such as Irresistin-16, and antisense oligonucleotides designed to disrupt the catalytic RNA component (Liu et al., 2020).

Other names

Ribonuclease PRNase PRNPrnpBrnpAtRNA-processing ribonuclease P

Inhibition of the catalytic RNA component or the protein-RNA interaction of the RNase P holoenzyme, preventing the 5'-end maturation of precursor tRNAs and thereby disrupting bacterial protein synthesis (Altman, 2007; Gopalan et al., 2018).