RNase ES ofStreptomyces coelicolorA3(2) Can Complement therneandrngMutations inEscherichia coli

Inagawa, Takabumi; Okamoto, Susumu; Wachi, Masaaki; Ochi, Kozo

doi:10.1271/bbb.67.1767

Cited by 5 publications

(10 citation statements)

References 24 publications

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“…Bottom, instability of psbA mRNA under darkness is caused post-transcription by RNases, which act on the AUbox (and SD) as targets. Scissor, endoribonuclease RNase E/G; packman, possible exoribonuclease larly, a Type III RNase E/G homologue of a Gram-positive bacterium, Streptomyces coelicolor A3(2), can also fulWll the functions of E. coli RNase E and RNase G (Inagawa et al 2003). Furthermore, a similar result was reported for the Type IV RNase E/G homologue of Aquifex aeolicus (Kaberdin and Bizebard 2005).…”

Section: Activity Domains Of Slr1129mentioning

confidence: 60%

Dark-induced mRNA instability involves RNase E/G-type endoribonuclease cleavage at the AU-box and SD sequences in cyanobacteria

et al. 2007

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Light-responsive gene expression is crucial to photosynthesizing organisms. Here, we studied functions of cis-elements (AU-box and SD sequences) and a trans-acting factor (ribonuclease, RNase) in light-responsive expression in cyanobacteria. The results indicated that AU-rich nucleotides with an AU-box, UAAAUAAA, just upstream from an SD confer instability on the mRNA under darkness. An RNase E/G homologue, Slr1129, of the cyanobacterium Synechocystis sp. strain PCC 6803 was purified and confirmed capable of endoribonucleolytic cleavage at the AU- (or AG)-rich sequences in vitro. The cleavage depends on the primary target sequence and secondary structure of the mRNA. Complementation tests using Escherichia coli rne/rng mutants showed that Slr1129 fulfilled the functions of both the RNase E and RNase G. An analysis of systematic mutations in the AU-box and SD sequences showed that the cis-elements also affect significantly mRNA stability in light-responsive genes. These results strongly suggested that dark-induced mRNA instability involves RNase E/G-type cleavage at the AU-box and SD sequences in cyanobacteria. The mechanical impact and a possible common mechanism with RNases for light-responsive gene expression are discussed.

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Section: Activity Domains Of Slr1129mentioning

confidence: 60%

Dark-induced mRNA instability involves RNase E/G-type endoribonuclease cleavage at the AU-box and SD sequences in cyanobacteria

et al. 2007

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“…It has also been reported that overproduction of the S. coelicolor RNase ES caused a severe growth defect in E. coli. 29) It is noteworthy that the expression patterns of cellular proteins changed drastically upon the expression of FL-NCgl2281 (Fig. 4).…”

Section: Discussionmentioning

confidence: 97%

“…37) These two studies suggest that the mycobacterial RNase E/G is functionally related to E. coli RNase E. S. coelicolor also has one RNase E/G homolog, which complemented both the E. coli rne-1 and the rng::cat mutation. 29,30) Bacillus subtilis has no RNase E/G homolog. It has RNase J instead.…”

Section: Discussionmentioning

confidence: 99%

“…Streptomyces coelicolor, which is taxonomically related to C. glutamicum, also has one RNase E/G homolog, named RNase ES, which can complement the rne and rng mutations in E. coli. 29,30) Though RNase ES itself is not essential for S. coelicolor growth, 30) it can rescue the temperature sensitivity of the E. coli rne-1 mutant. 29) Furthermore, RNase ES interacts with PNPase, suggesting the existence of the E. coli degradosome-like complex in S. coelicolor.…”

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confidence: 99%

“…29,30) Though RNase ES itself is not essential for S. coelicolor growth, 30) it can rescue the temperature sensitivity of the E. coli rne-1 mutant. 29) Furthermore, RNase ES interacts with PNPase, suggesting the existence of the E. coli degradosome-like complex in S. coelicolor. 30) In this study, we cloned and expressed the C. glutamicum NCgl2281 gene encoding an RNase E/G family endoribonuclease in E. coli and examined its complementation ability as to E. coli rne-1 and rng::cat mutations.…”

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TheCorynebacterium glutamicumNCgl2281 Gene Encoding an RNase E/G Family Endoribonuclease Can Complement theEscherichia coli rng::catMutation but Not therne-1Mutation

Maeda

Sakai

Wachi

2009

Bioscience, Biotechnology, and Biochemistry

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The Corynebacterium glutamicum NCgl2281 gene encodes an RNase E/G family endoribonuclease having an additional N-terminal domain of unknown function. In this study, we constructed plasmids expressing the full length (FL) and the N-terminally truncated form (ÁN) of NCgl2281 and examined their complementation ability as to Escherichia coli rng::cat and rne-1 mutations. Both FL-and ÁN-NCgl2281 rescued the defects caused by the rng::cat mutation, i.e., accumulation of 16S rRNA precursor, overproduction of the AdhE protein, and growth inhibition on M9 glucose medium. On the other hand, they did not complement the rne-1 mutation. These results indicate that the C. glutamicum NCgl2281 endoribonuclease is functionally more closely related to the E. coli RNase G than to RNase E.

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Guanosine 5′‐diphosphate 3′‐diphosphate (ppGpp) as a negative modulator of polynucleotide phosphorylase activity in a ‘rare’ actinomycete

Siculella¹,

Damiano²,

Summa³

et al. 2010

Molecular Microbiology

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SummaryWith the beginning of the idiophase the highly phosphorylated guanylic nucleotides guanosine 5Ј-diphosphate 3Ј-diphosphate (ppGpp) and guanosine 5Ј-triphosphate 3Ј-diphosphate (pppGpp), collectively referred to as (p)ppGpp, activate stress survival adaptation programmes and trigger secondary metabolism in actinomycetes. The major target of (p)ppGpp is the RNA polymerase, where it binds altering the enzyme activity. In this study analysis of the polynucleotide phosphorylase (PNPase)-encoding gene pnp mRNA, in Nonomuraea sp. ATCC 39727 wild-type, constitutively stringent and relaxed strains, led us to hypothesize that in actinomycetes (p)ppGpp may modulate gene expression at the level of RNA decay also. This hypothesis was supported by: (i) in vitro evidence that ppGpp, at physiological levels, inhibited both polynucleotide polymerase and phosphorolytic activities of PNPase in Nonomuraea sp., but not in Escherichia coli, (ii) in vivo data showing that the pnp mRNA and the A40926 antibiotic clusterspecific dpgA mRNA were stabilized during the idiophase in the wild-type strain but not in a relaxed mutant and (iii) measurement of chemical decay of pulse-labelled bulk mRNA. The results of biochemical tests suggest competitive inhibition of ppGpp with respect to nucleoside diphosphates in polynucleotide polymerase assays and mixed inhibition with respect to inorganic phosphate when the RNA phosphorolytic activity was determined.

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RNase ES ofStreptomyces coelicolorA3(2) Can Complement therneandrngMutations inEscherichia coli

Cited by 5 publications

References 24 publications

Dark-induced mRNA instability involves RNase E/G-type endoribonuclease cleavage at the AU-box and SD sequences in cyanobacteria

Dark-induced mRNA instability involves RNase E/G-type endoribonuclease cleavage at the AU-box and SD sequences in cyanobacteria

TheCorynebacterium glutamicumNCgl2281 Gene Encoding an RNase E/G Family Endoribonuclease Can Complement theEscherichia coli rng::catMutation but Not therne-1Mutation

Guanosine 5′‐diphosphate 3′‐diphosphate (ppGpp) as a negative modulator of polynucleotide phosphorylase activity in a ‘rare’ actinomycete

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