Corynebacterium glutamicum RNase E/G-type endoribonuclease encoded by NCgl2281 is involved in the 5′ maturation of 5S rRNA

Maeda, Tomoya; Wachi, Masaaki

doi:10.1007/s00203-011-0728-3

Cited by 8 publications

(13 citation statements)

References 57 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A previous study suggested that C. glutamicum RNase E/G was more closely related to E. coli RNase G than to RNase E (36). We then showed that RNase E/G is involved in the processing of 5S rRNA, although it is not essential for cell viability (37). Here we show that RNase E/G is a novel posttranscriptional regulator of the glyoxylate cycle in C. glutamicum.…”

mentioning

confidence: 69%

“…Total cellular RNA from C. glutamicum ATCC 31831 and D2281 was isolated as described previously (37). Briefly, overnight cultures grown on CGC minimal medium containing 1% glucose at 30°C were washed and then inoculated into fresh CGC minimal medium containing 1% sodium acetate.…”

Section: Methodsmentioning

confidence: 99%

“…Primer extension analysis was performed as described previously (37). Briefly, the 5= end of aceA mRNA was determined by nonradioactive primer extension analysis.…”

Section: Methodsmentioning

confidence: 99%

See 2 more Smart Citations

3′ Untranslated Region-Dependent Degradation of the aceA mRNA, Encoding the Glyoxylate Cycle Enzyme Isocitrate Lyase, by RNase E/G in Corynebacterium glutamicum

Maeda

Wachi

2012

Appl Environ Microbiol

Self Cite

View full text Add to dashboard Cite

We previously reported that the Corynebacterium glutamicum RNase E/G encoded by the rneG gene (NCgl2281) is required for the 5= maturation of 5S rRNA. In the search for the intracellular target RNAs of RNase E/G other than the 5S rRNA precursor, we detected that the amount of isocitrate lyase, an enzyme of the glyoxylate cycle, increased in rneG knockout mutant cells grown on sodium acetate as the sole carbon source. Rifampin chase experiments showed that the half-life of the aceA mRNA was about 4 times longer in the rneG knockout mutant than in the wild type. Quantitative real-time PCR analysis also confirmed that the level of aceA mRNA was approximately 3-fold higher in the rneG knockout mutant strain than in the wild type. Such differences were not observed in other mRNAs encoding enzymes involved in acetate metabolism. Analysis by 3= rapid amplification of cDNA ends suggested that RNase E/G cleaves the aceA mRNA at a single-stranded AU-rich region in the 3= untranslated region (3=-UTR). The lacZ fusion assay showed that the 3=-UTR rendered lacZ mRNA RNase E/G dependent. These findings indicate that RNase E/G is a novel regulator of the glyoxylate cycle in C. glutamicum.

show abstract

mentioning

confidence: 69%

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

3′ Untranslated Region-Dependent Degradation of the aceA mRNA, Encoding the Glyoxylate Cycle Enzyme Isocitrate Lyase, by RNase E/G in Corynebacterium glutamicum

Maeda

Wachi

2012

Appl Environ Microbiol

Self Cite

View full text Add to dashboard Cite

show abstract

“…A suicide vector, pCRA725, carrying the sacB gene was used for markerless gene deletion and gene modification (33). Using plasmids LKSΔrnZ, LKSΔybeY, and LKSΔrnR and C. glutamicum strain R as a wild type, ΔrnZ, ΔybeY, and ΔrnR strains were constructed by two-step homologous recombination, as described previously (34). The DNA fragment encoding the ffh gene fused with a FLAG tag (DYKDDDK) was cloned into plasmid pCRA725 (33), yielding LKSffh-FLAG.…”

Section: Fĭ-flagmentioning

confidence: 99%

“…Northern hybridization was performed as described previously (34). A digoxigenin (DIG)-labeled antisense RNA probe targeting the 4.5S RNA coding region (entire 4.5S RNA probe) and the 3= spacer region (3= spacer region-specific RNA probe) was produced according to the manufacturer's instructions (Roche).…”

Section: Fĭ-flagmentioning

confidence: 99%

Polynucleotide Phosphorylase, RNase E/G, and YbeY Are Involved in the Maturation of 4.5S RNA in Corynebacterium glutamicum

et al. 2017

Self Cite

View full text Add to dashboard Cite

Corynebacterium glutamicum has been applied for the industrial production of various metabolites, such as amino acids. To understand the biosynthesis of the membrane protein in this bacterium, we investigated the process of signal recognition particle (SRP) assembly. SRP is found in all three domains of life and plays an important role in the membrane insertion of proteins. SRP RNA is initially transcribed as precursor molecules; however, relatively little is known about its maturation. In C. glutamicum, SRP consists of the Ffh protein and 4.5S RNA lacking an Alu domain. In this study, we found that 3=-to-5= exoribonuclease, polynucleotide phosphorylase (PNPase), and two endo-type RNases, RNase E/G and YbeY, are involved in the 3= maturation of 4.5S RNA in C. glutamicum. The mature form of 4.5S RNA was inefficiently formed in ΔrneG Δpnp mutant cells, suggesting the existence of an alternative pathway for the 3= maturation of 4.5S RNA. Primer extension analysis also revealed that the 5= mature end of 4.5S RNA corresponds to that of the transcriptional start site. Immunoprecipitated Ffh protein contained immature 4.5S RNA in Δpnp, ΔrneG, and ΔybeY mutants, suggesting that 4.5S RNA precursors can interact with Ffh. These results imply that the maturation of 4.5S RNA can be performed in the 4.5S RNA-Ffh complex.IMPORTANCE Overproduction of a membrane protein, such as a transporter, is useful for engineering of strains of Corynebacterium glutamicum, which is a workhorse of amino acid production. To understand membrane protein biogenesis in this bacterium, we investigated the process of signal recognition particle (SRP) assembly. SRP contains the Ffh protein and SRP RNA and plays an important role in the membrane insertion of proteins. Although SRP RNA is highly conserved among the three domains of life, relatively little is known about its maturation. We show that PNPase, RNase E/G, and YbeY are involved in the 3= maturation of the SRP RNA (4.5S RNA) in this bacterium. This indicates that 3= end processing in this organism is different from that in other bacteria, such as Escherichia coli.

show abstract

Translation | Pre-tRNA and Pre-rRNA Processing in Bacteria

2021

Encyclopedia of Biological Chemistry III

View full text Add to dashboard Cite

Corynebacterium glutamicum RNase E/G-type endoribonuclease encoded by NCgl2281 is involved in the 5′ maturation of 5S rRNA

Cited by 8 publications

References 57 publications

3′ Untranslated Region-Dependent Degradation of the aceA mRNA, Encoding the Glyoxylate Cycle Enzyme Isocitrate Lyase, by RNase E/G in Corynebacterium glutamicum

3′ Untranslated Region-Dependent Degradation of the aceA mRNA, Encoding the Glyoxylate Cycle Enzyme Isocitrate Lyase, by RNase E/G in Corynebacterium glutamicum

Polynucleotide Phosphorylase, RNase E/G, and YbeY Are Involved in the Maturation of 4.5S RNA in Corynebacterium glutamicum

Translation | Pre-tRNA and Pre-rRNA Processing in Bacteria

Contact Info

Product

Resources

About