Identification of the gene encoding the 5S ribosomal RNA maturase in Bacillus subtilis: Mature 5S rRNA is dispensable for ribosome function

Condon, Ciarán; Bréchemier-Baey, Dominique; Beltchev, B.; Grunberg‐Manago, Marianne; Putzer, Harald

doi:10.1017/s1355838201002163

Cited by 53 publications

(62 citation statements)

References 39 publications

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“…These strains have long lag times that increase with increasing time spent in stationary phase (H. Putzer and C. Condon, unpublished results). No mature 5S rRNA whatsoever can be detected in ⌬rnmV strains, showing that no other enzyme can take the place of RNase M5 (43). Precursor 5S rRNA molecules accumulate in both ribosomes and polysomes, suggesting that maturation of 5S rRNA is dispensable for ribosome function in B. subtilis at least.…”

Section: The Endoribonucleasesmentioning

confidence: 96%

“…High concentrations of ribosomal protein L5, which also binds 5S rRNA, inhibit the cleavage reaction (218). RNase M5 has been estimated to be present at about 100 molecules per B. subtilis cell (43,184). The enzyme was purified to homogeneity almost 20 years ago and estimated to be about 24 kDa in size (182).…”

Section: The Endoribonucleasesmentioning

confidence: 99%

“…However, its gene was only recently identified. RNase M5 was repurified from B. subtilis, and after considerable difficulty in separating it from ribosomal protein L6, sufficient material was obtained to sequence its N terminus and identify its gene (43). The RNase M5 gene was one of previously unknown function, yabF, and was renamed rnmV.…”

Section: The Endoribonucleasesmentioning

confidence: 99%

“…Only members Clostridium and Listeria species and Bacillus halodurans have both types of 5S rRNA maturases (44). Both enzymes are capable of processing Clostridium difficile 5S rRNA in vitro (43).…”

Section: The Endoribonucleasesmentioning

confidence: 99%

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RNA Processing and Degradation inBacillus subtilis

Condon

2003

Microbiol Mol Biol Rev

141

134

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This review focuses on the enzymes and pathways of RNA processing and degradation in Bacillus subtilis, and compares them to those of its gram-negative counterpart, Escherichia coli. A comparison of the genomes from the two organisms reveals that B. subtilis has a very different selection of RNases available for RNA maturation. Of 17 characterized ribonuclease activities thus far identified in E. coli and B. subtilis, only 6 are shared, 3 exoribonucleases and 3 endoribonucleases. Some enzymes essential for cell viability in E. coli, such as RNase E and oligoribonuclease, do not have homologs in B. subtilis, and of those enzymes in common, some combinations are essential in one organism but not in the other. The degradation pathways and transcript half-lives have been examined to various degrees for a dozen or so B. subtilis mRNAs. The determinants of mRNA stability have been characterized for a number of these and point to a fundamentally different process in the initiation of mRNA decay. While RNase E binds to the 5′ end and catalyzes the rate-limiting cleavage of the majority of E. coli RNAs by looping to internal sites, the equivalent nuclease in B. subtilis, although not yet identified, is predicted to scan or track from the 5′ end. RNase E can also access cleavage sites directly, albeit less efficiently, while the enzyme responsible for initiating the decay of B. subtilis mRNAs appears incapable of direct entry. Thus, unlike E. coli, RNAs possessing stable secondary structures or sites for protein or ribosome binding near the 5′ end can have very long half-lives even if the RNA is not protected by translation

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Section: The Endoribonucleasesmentioning

confidence: 96%

Section: The Endoribonucleasesmentioning

confidence: 99%

Section: The Endoribonucleasesmentioning

confidence: 99%

Section: The Endoribonucleasesmentioning

confidence: 99%

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RNA Processing and Degradation inBacillus subtilis

Condon

2003

Microbiol Mol Biol Rev

141

134

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“…The endonucleolytic step also occurs in bacteria. In B. subtilis, it is carried out by RNase M5, which cleaves a dsRNA moiety in the 5S rRNA precursor (Condon et al 2001). In E. coli, the substrate is a single-stranded segment that is cleaved by RNase E (Ghora and Apirion 1978), followed by 39 trimming by the exoribonuclease RNase T (Li and Deutscher 1995).…”

Section: In Vitro Dissection Of As5 Inhibitor Sequencesmentioning

confidence: 99%

Overaccumulation of the chloroplast antisense RNA AS5 is correlated with decreased abundance of 5S rRNA in vivo and inefficient 5S rRNA maturation in vitro

Sharwood¹,

Hotto²,

Bollenbach³

et al. 2010

RNA

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Post-transcriptional regulation in the chloroplast is exerted by nucleus-encoded ribonucleases and RNA-binding proteins. One of these ribonucleases is RNR1, a 39-to-59 exoribonuclease of the RNase II family. We have previously shown that Arabidopsis rnr1-null mutants exhibit specific abnormalities in the expression of the rRNA operon, including the accumulation of precursor 23S, 16S, and 4.5S species and a concomitant decrease in the mature species. 5S rRNA transcripts, however, accumulate to a very low level in both precursor and mature forms, suggesting that they are unstable in the rnr1 background. Here we demonstrate that rnr1 plants overaccumulate an antisense RNA, AS5, that is complementary to the 5S rRNA, its intergenic spacer, and the downstream trnR gene, which encodes tRNA Arg , raising the possibility that AS5 destabilizes 5S rRNA or its precursor and/or blocks rRNA maturation. To investigate this, we used an in vitro system that supports 5S rRNA and trnR processing. We show that AS5 inhibits 5S rRNA maturation from a 5S-trnR precursor, and shorter versions of AS5 demonstrate that inhibition requires intergenic sequences. To test whether the sense and antisense RNAs form double-stranded regions in vitro, treatment with the single-strand-specific mung bean nuclease was used. These results suggest that 5S-AS5 duplexes interfere with a sense-strand secondary structure near the endonucleolytic cleavage site downstream from the 5S rRNA coding region. We hypothesize that these duplexes are degraded by a dsRNA-specific ribonuclease in vivo, contributing to the 5S rRNA deficiency observed in rnr1.

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mRNA Decay and RNA‐Degrading Machines in Prokaryotes and Eukaryotes

Carpousis

Dreyfus

2004

Protein Synthesis and Ribosome Structure

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Identification of the gene encoding the 5S ribosomal RNA maturase in Bacillus subtilis: Mature 5S rRNA is dispensable for ribosome function

Cited by 53 publications

References 39 publications

RNA Processing and Degradation inBacillus subtilis

RNA Processing and Degradation inBacillus subtilis

Overaccumulation of the chloroplast antisense RNA AS5 is correlated with decreased abundance of 5S rRNA in vivo and inefficient 5S rRNA maturation in vitro

mRNA Decay and RNA‐Degrading Machines in Prokaryotes and Eukaryotes

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