Version 1
: Received: 8 July 2024 / Approved: 9 July 2024 / Online: 9 July 2024 (13:44:51 CEST)
How to cite:
Laalami, S.; Cavaiuolo, M.; Oberto, J.; Putzer, H. Membrane Localization of RNase Y Is Important for Global Gene Expression in Bacillus subtilis. Preprints2024, 2024070751. https://doi.org/10.20944/preprints202407.0751.v1
Laalami, S.; Cavaiuolo, M.; Oberto, J.; Putzer, H. Membrane Localization of RNase Y Is Important for Global Gene Expression in Bacillus subtilis. Preprints 2024, 2024070751. https://doi.org/10.20944/preprints202407.0751.v1
Laalami, S.; Cavaiuolo, M.; Oberto, J.; Putzer, H. Membrane Localization of RNase Y Is Important for Global Gene Expression in Bacillus subtilis. Preprints2024, 2024070751. https://doi.org/10.20944/preprints202407.0751.v1
APA Style
Laalami, S., Cavaiuolo, M., Oberto, J., & Putzer, H. (2024). Membrane Localization of RNase Y Is Important for Global Gene Expression in Bacillus subtilis. Preprints. https://doi.org/10.20944/preprints202407.0751.v1
Chicago/Turabian Style
Laalami, S., Jacques Oberto and Harald Putzer. 2024 "Membrane Localization of RNase Y Is Important for Global Gene Expression in Bacillus subtilis" Preprints. https://doi.org/10.20944/preprints202407.0751.v1
Abstract
Abstract: RNase Y is an endoribonuclease that governs global mRNA turnover/processing in Ba-cillus subtilis and likely many other bacteria. The enzyme is anchored at the cell membrane, a pseudo-compartmentalization that appears coherent with its task to initiate decay of mRNAs translated predominantly at the cell periphery. However, the reason and consequence for RNase Y attachment to the membrane are largely unknown. We have studied a strain expressing wild-type levels of a cytoplasmic form of RNase Y from the chromosomal locus. This strain exhibits a slow growth phenotype similar to an RNase Y null mutant. Genome-wide data show a significant effect on the expression of hundreds of genes. Certain RNA substrates clearly require RNase Y membrane attachment but others do not. We found no correlation between mRNA stabilization and the cellular location or function of encoded proteins. The Y-complex, an RNase Y specificity factor, appears to also recognize the cytoplasmic form of the enzyme which is able to restore wild-type levels of the corresponding transcripts. We propose that membrane attachment of RNase Y is required for the functional interaction with many coding and non-coding RNAs, for limiting the cleavage of certain substrates and potentially to avoid unfavorable competition between RNase Y and other ribonucleases like RNase J that have a similar evolutionarily conserved cleavage speci-ficity.
Biology and Life Sciences, Biochemistry and Molecular Biology
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
