Shut down of multidrug transporter bmrCD mRNA expression mediated by the ribosome associated endoribonuclease Rae1 cleavage in a new cryptic ORF
- Valentin Deves1,
- Aude Trinquier2,
- Laetitia Gilet3,
- Jawad Alharake1,
- Ciaran Condon3 and
- Frederique Braun1,4
- ↵* Corresponding author; email: braun{at}ibpc.fr
Abstract
Rae1 is a well-conserved endoribonuclease among Gram-positive bacteria, cyanobacteria and the chloroplasts of higher plants. We have previously shown that Rae1 cleaves the Bacillus subtilis yrzI operon mRNA in a translation-dependent manner within a short open reading frame (ORF) called S1025, encoding a 17-amino acid (aa) peptide of unknown function. Here, we map a new Rae1 cleavage site in the bmrBCD operon mRNA encoding a multidrug transporter, within a unannotated 26-aa cryptic ORF that we have named bmrX. Expression of the bmrCD portion of the mRNA is ensured by an antibiotic dependent ribosome attenuation mechanism within the upstream ORF bmrB. Cleavage by Rae1 within bmrX supresses bmrCD expression that escapes attenuation control in the absence of antibiotics. Similar to S1025, Rae1 cleavage within bmrX is both translation- and reading frame-dependent. Consistent with this, we show that translation-dependent cleavage by Rae1 promotes ribosome rescue by the tmRNA.
Keywords
- Received April 19, 2023.
- Accepted April 21, 2023.
- Published by Cold Spring Harbor Laboratory Press for the RNA Society
This article is distributed exclusively by the RNA Society for the first 12 months after the full-issue publication date (see http://rnajournal.cshlp.org/site/misc/terms.xhtml). After 12 months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.
