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Quasi-essentiality of RNase Y inBacillus subtilisis caused by its critical role in the control of mRNA homeostasis
- Source :
- Nucleic Acids Research
- Publication Year :
- 2021
- Publisher :
- Oxford University Press (OUP), 2021.
-
Abstract
- RNA turnover is essential in all domains of life. The endonuclease RNase Y (rny) is one of the key components involved in RNA metabolism of the model organism Bacillus subtilis. Essentiality of RNase Y has been a matter of discussion, since deletion of the rny gene is possible, but leads to severe phenotypic effects. In this work, we demonstrate that the rny mutant strain rapidly evolves suppressor mutations to at least partially alleviate these defects. All suppressor mutants had acquired a duplication of an about 60 kb long genomic region encompassing genes for all three core subunits of the RNA polymerase—α, β, β′. When the duplication of the RNA polymerase genes was prevented by relocation of the rpoA gene in the B. subtilis genome, all suppressor mutants carried distinct single point mutations in evolutionary conserved regions of genes coding either for the β or β’ subunits of the RNA polymerase that were not tolerated by wild type bacteria. In vitro transcription assays with the mutated polymerase variants showed a severe decrease in transcription efficiency. Altogether, our results suggest a tight cooperation between RNase Y and the RNA polymerase to establish an optimal RNA homeostasis in B. subtilis cells.
- Subjects :
- Transcription, Genetic
AcademicSubjects/SCI00010
RNase P
Mutant
Evolution, Molecular
03 medical and health sciences
chemistry.chemical_compound
Suppression, Genetic
Transcription (biology)
Gene Duplication
RNA polymerase
Endoribonucleases
RNA and RNA-protein complexes
Genetics
Homeostasis
RNA, Messenger
Gene
Polymerase
030304 developmental biology
0303 health sciences
Messenger RNA
biology
030306 microbiology
RNA
DNA-Directed RNA Polymerases
chemistry
Genes, Bacterial
Mutation
biology.protein
Transcriptome
Gene Deletion
Bacillus subtilis
Subjects
Details
- ISSN :
- 13624962 and 03051048
- Volume :
- 49
- Database :
- OpenAIRE
- Journal :
- Nucleic Acids Research
- Accession number :
- edsair.doi.dedup.....daae2300b9d95412cf981a95e11039d2
- Full Text :
- https://doi.org/10.1093/nar/gkab528