{Reference Type}: Journal Article
{Title}: Critical factors for precise and efficient RNA cleavage by RNase Y in Staphylococcus aureus.
{Author}: Le Scornet A;Jousselin A;Baumas K;Kostova G;Durand S;Poljak L;Barriot R;Coutant E;Pigearias R;Tejero G;Lootvoet J;Péllisier C;Munoz G;Condon C;Redder P;
{Journal}: PLoS Genet
{Volume}: 20
{Issue}: 8
{Year}: 2024 Aug 1
暂无{DOI}: 10.1371/journal.pgen.1011349
{Abstract}: Cellular processes require precise and specific gene regulation, in which continuous mRNA degradation is a major element. The mRNA degradation mechanisms should be able to degrade a wide range of different RNA substrates with high efficiency, but should at the same time be limited, to avoid killing the cell by elimination of all cellular RNA. RNase Y is a major endoribonuclease found in most Firmicutes, including Bacillus subtilis and Staphylococcus aureus. However, the molecular interactions that direct RNase Y to cleave the correct RNA molecules at the correct position remain unknown. In this work we have identified transcripts that are homologs in S. aureus and B. subtilis, and are RNase Y targets in both bacteria. Two such transcript pairs were used as models to show a functional overlap between the S. aureus and the B. subtilis RNase Y, which highlighted the importance of the nucleotide sequence of the RNA molecule itself in the RNase Y targeting process. Cleavage efficiency is driven by the primary nucleotide sequence immediately downstream of the cleavage site and base-pairing in a secondary structure a few nucleotides downstream. Cleavage positioning is roughly localised by the downstream secondary structure and fine-tuned by the nucleotide immediately upstream of the cleavage. The identified elements were sufficient for RNase Y-dependent cleavage, since the sequence elements from one of the model transcripts were able to convert an exogenous non-target transcript into a target for RNase Y.