Work

The endoribonuclease Rae1 from B acillus subtilis cleaves mRNA upstream of stalled ribosomes

Year: 2025

Type: article

Abstract: The ribosome-associated endoribonuclease 1 (Rae1) cleaves messenger RNAs (mRNAs) in a translation-dependent manner. Here, we identify a new Rae1 target, the fliY mRNA, which is cleaved by Rae1 in the absence of the elongation factor P. The Rae1 site was mapped 12 nucleotides upstream of the second proline codon of an SPP stalling motif in fliY. Remarkably, Rae1 cleavages also occur 12 nucleotides upstream of the stop codon within two validated Rae1 mRNA targets, bmrX and spyA (S1025). Shifting the stop codon relative to the Rae1 cutting site abolished Rae1 sensitivity of bmrX and spyA mRNAs. We show that ribosome pausing occurs at the spyA stop codon, confirming its crucial role, and positioning the Rae1 cleavage at the tail end of the stalled ribosome, rather than in the A-site as previously proposed. These findings reveal a compelling novel mechanism by which Rae1 mediates mRNA cleavage in coordination with immobile ribosomes.

Source: Nucleic Acids Research

DOI: 10.1093/nar/gkaf843

Authors: Valentin Deves, Alexandre D’Halluin, Laëtitia Gilet, Ciarán Condon, Frédérique Braun

Institutions: Centre National de la Recherche Scientifique, Université Paris Cité, Institut de Biologie Physico-Chimique, Expression Génétique Microbienne

Language: English

Topic: RNA and protein synthesis mechanisms

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: gold

Estimated APC paid: $3,992

Funders: Equipex, Agence Nationale de la Recherche, Centre National de la Recherche Scientifique, College of Natural Resources and Sciences, Humboldt State University