Determinant role of E. coli RNase III in the decay of both specific and heterologous mRNAs

Santos, Jorge M.; Drider, Djamel; Marujo, Paulo E.; López, Paloma; Arraiano, Cecıćlia Maria

doi:10.1111/j.1574-6968.1997.tb12749.x

Cited by 17 publications

(8 citation statements)

References 15 publications

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“…RNase III participates as a stress response modulator, controlling the steady-state levels of genes involved in cellular adaptation to stress (Santos et al, 1997;Freire et al, 2006;Sim et al, 2010). It was seen in Salmonella typhimur-ium that RNase III regulates the levels of the sRNA MicA (Viegas et al, 2007), a main regulator of the abundant outer membrane protein OmpA that plays an important structural role in the cell and is involved in pathogenesis (Guillier et al, 2006).…”

Section: Rnase IIImentioning

confidence: 99%

The critical role of RNA processing and degradation in the control of gene expression

et al. 2010

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The continuous degradation and synthesis of prokaryotic mRNAs not only give rise to the metabolic changes that are required as cells grow and divide but also rapid adaptation to new environmental conditions. In bacteria, RNAs can be degraded by mechanisms that act independently, but in parallel, and that target different sites with different efficiencies. The accessibility of sites for degradation depends on several factors, including RNA higher-order structure, protection by translating ribosomes and polyadenylation status. Furthermore, RNA degradation mechanisms have shown to be determinant for the post-transcriptional control of gene expression. RNases mediate the processing, decay and quality control of RNA. RNases can be divided into endonucleases that cleave the RNA internally or exonucleases that cleave the RNA from one of the extremities. Just in Escherichia coli there are >20 different RNases. RNase E is a single-strand-specific endonuclease critical for mRNA decay in E. coli. The enzyme interacts with the exonuclease polynucleotide phosphorylase (PNPase), enolase and RNA helicase B (RhlB) to form the degradosome. However, in Bacillus subtilis, this enzyme is absent, but it has other main endonucleases such as RNase J1 and RNase III. RNase III cleaves double-stranded RNA and family members are involved in RNA interference in eukaryotes. RNase II family members are ubiquitous exonucleases, and in eukaryotes, they can act as the catalytic subunit of the exosome. RNases act in different pathways to execute the maturation of rRNAs and tRNAs, and intervene in the decay of many different mRNAs and small noncoding RNAs. In general, RNases act as a global regulatory network extremely important for the regulation of RNA levels.

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Section: Rnase IIImentioning

confidence: 99%

The critical role of RNA processing and degradation in the control of gene expression

et al. 2010

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“…The bolA1p promoter is also induced in the exponential phase in response to several stresses, such as heat, acid, oxidative, osmotic, and glucose depletion [3,32]. At the post-transcriptional level, BolA is indirectly modulated by ribonuclease III, which increases rpoS mRNA and σ S protein levels [11,30]. Polyadenylation has been shown to reduce σ S proteolysis, and consequently affects bolA [31].…”

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confidence: 99%

Characterization of the BolA Homolog IbaG: A New Gene Involved in Acid Resistance

Guinote¹,

Moreira

Freire³

et al. 2012

J. Microbiol. Biotechnol.

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BolA protein homologs are widely distributed in nature. In this report, we have studied for the first time YrbA, the only BolA homolog present in Escherichia coli, which we have renamed ibaG. We have constructed single and multiple ibaG mutants, and overexpressed ibaG in wildtype strains, in order to characterize this gene. The ibaG phenotypes are different from the bolA-associated round morphologies or growth profiles. Interestingly, ibaG and bolA single-and double-deletion mutants grow faster and have higher viabilities in rich media, whereas the overexpressed strains are significantly growth impaired. However, the mutant strains have lower viabilities than the wild type in the late stationary phase, indicating that both bolA and ibaG are important for survival in difficult growth conditions. bolA, as a transcription factor, binds to some promoters, but ibaG does not interact with the same DNA regions. We have determined that ibaG is transcribed in an operon with the murA gene, involved in the synthesis of peptidoglycan precursors. ibaG was also seen to change its mRNA expression pattern in response to acidic stress. ibaG may thus represent a new gene involved in cell resistance against acid stress.

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“…The complexity of bolA regulation probably results from the fact that this gene is necessary for efficient adaptation to both bountiful and starving growth conditions (Santos et al ., 1997; 1999; 2002; Vieira et al ., 2004). In this report we show that the bolA1 p mRNA is more stable when there is more transcription driven by Eσ S in response to depletion of glucose.…”

Section: Discussionmentioning

confidence: 99%

“…Strains used were E. coli MG1693 ( thyA715 ) (Bachmann and Low, 1980), SK7988 ( thyA715 pcnB ) (O’Hara et al ., 1995), SK5704 ( thyA715 ams‐1/rne‐1, rnb‐500, pnp‐7 ) (Arraiano et al ., 1988), CMA10 (MG1693 transformed with pMAK580) (Santos et al ., 1997) and CMA307 – this work ( ams‐1/rne‐1, rnb‐500, pnp‐7, pcnB ) . CMA307 was constructed by P1 transduction of pcnB from SK7988 to strain SK5704.…”

Section: Methodsmentioning

confidence: 99%

Poly(A)‐polymerase I links transcription with mRNA degradation via σ^S proteolysis

Santos

Freire

Mesquita

et al. 2006

Molecular Microbiology

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SummaryBacteria rapidly adapt to changes in growth conditions through control of transcription and specific mRNA degradation. Interplay of both mechanisms must exist in order to achieve fine-tuned regulation of gene expression. Transcription of the Escherichia coli bolA gene is mediated by the RpoS/ σ σ σ σ S transcription factor in response to environmental signals. In this report it is shown that the mechanisms of bolA1p mRNA transcription and degradation are tightly connected at the onset of stationary phase and in response to sudden carbon starvation. In stationary phase, bolA1p mRNA levels were reduced 2.5-fold in a poly(A)-polymerase I (PAPI) mutant, explained by the significant threefold reduction in σ σ σ σ S protein levels in the same strain. Furthermore, fusions with the rpoS gene, analysis of the stability of σ σ σ σ S and the levels of RssB indicate that the absence of PAPI enhances RssB-mediated σ σ σ σ S proteolysis specifically in starved cells. The fact that PAPI induces higher cellular levels of a global regulator is a novel finding of wide biological significance. PAPI could work as a linker between transcription and mRNA degradation with the ultimate goal of adapting and surviving to growth-limiting conditions.

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Determinant role of E. coli RNase III in the decay of both specific and heterologous mRNAs

Cited by 17 publications

References 15 publications

The critical role of RNA processing and degradation in the control of gene expression

The critical role of RNA processing and degradation in the control of gene expression

Characterization of the BolA Homolog IbaG: A New Gene Involved in Acid Resistance

Poly(A)‐polymerase I links transcription with mRNA degradation via σ^S proteolysis

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Determinant role of E. coli RNase III in the decay of both specific and heterologous mRNAs

Cited by 17 publications

References 15 publications

The critical role of RNA processing and degradation in the control of gene expression

The critical role of RNA processing and degradation in the control of gene expression

Characterization of the BolA Homolog IbaG: A New Gene Involved in Acid Resistance

Poly(A)‐polymerase I links transcription with mRNA degradation via σS proteolysis

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Poly(A)‐polymerase I links transcription with mRNA degradation via σ^S proteolysis