RNase PH is a tRNA nucleotidyltransferase, present in archaea and bacteria, that is involved in tRNA processing. Contrary to hydrolytic enzymes, it is a phosphorolytic enzyme, meaning that …

RNase PH (EC 2.7.7.56) is a second Pi-dependent 3′ → 5′ exoribonuclease in bacteria that functions in the trimming of the tRNA precursors at their 3′ ends [18]. In bacteria, six RNase …

After RNase T, RNase PH is most effective in supporting the growth of cells lacking multiple exoribonucleases (Kelly and Deutscher 1992b), indicating that RNase PH can take over the …

RNase PH is a 3′–5′ phosphorolytic exoribonuclease that participates in the maturation of tRNA and degradation of structured RNAs (Deutscher 1990; Jain 2012).

RNase PH has a molecular mass of 45-50 kDa and favors tRNA precursors as substrates. The possible physiological role of RNase PH and the advantages of phosphorolytic processing are …

Mar 8, 2022 · The eukaryotic exosome core is composed of six individually encoded RNase PH-like subunits, but it is not a phosphorolytic enzyme per se; it directly associates with Rrp44 and …

The dissociated RNase PH dimer completely lost its binding affinity and catalytic activity against a precursor tRNA. Our structural and mutational analyses of RNase PH demonstrate that the …

RNase P is one of two known multiple turnover ribozymes in nature (the other being the ribosome). In bacteria RNase P is also responsible for the catalytic activity of holoenzymes, …

RNase PH forms a homo-hexameric ring composed of PH subunits (A). In PNPase, each monomer consists of a PH1 and a PH2 domain with two RNA-binding domains, S1 and KH (B).

Overall, these results indicate that RNase PH plays a novel role in the degradation of structured RNAs and provides a potential explanation for the growth defects caused by an absence of the …