RNase Y, a novel endoribonuclease, initiates riboswitch turnover in Bacillus subtilis

Shahbabian, Karen; Jamalli, Ailar; Zig, Léna; Putzer, Harald

doi:10.1038/emboj.2009.283

Cited by 219 publications

(395 citation statements)

References 39 publications

(78 reference statements)

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“…A model in which RNase Y processing occurs through a 6 nt (from the structure) ruler and cut mechanism was proposed. A similar scenario was previously observed in B. subtilis , where RNase Y processes the yitJ riboswitch, 6 nt upstream of the aptamer structure [12]. In speB mRNA, RNase Y processing events were 6 nt apart, however as mentioned above in a poorly structured region, and thus it would be unlikely that the ruler and cut mechanism by RNase Y is applicable for speB mRNA in S. pyogenes .…”

Section: Resultssupporting

confidence: 66%

“…Although previous studies showed that RNase Y is sensitive to secondary structures located downstream of the processing events [10,12], a recent transcriptomic analysis in B. subtilis did not identify any consensus motif (neither sequence nor RNA structure) in proximity of RNase Y cleavages [39]. Our mutational study indicates that the sequence requirement ( i.e .…”

Section: Discussioncontrasting

confidence: 58%

“…In some of the RNase Y targets described, the processing was shown to occur in proximity of RNA structures and in adenosine/uridine rich regions [10,12]. For instance, RNase Y cleaves the yitJ riboswitch and the sae mRNA operon upstream of double-stranded RNA structures, in Bacillus subtilis and S. aureus respectively [10,12].…”

Section: Introductionmentioning

confidence: 99%

“…For instance, RNase Y cleaves the yitJ riboswitch and the sae mRNA operon upstream of double-stranded RNA structures, in Bacillus subtilis and S. aureus respectively [10,12]. In S. aureus , RNase Y processing events were found preferentially after a guanosine (G) [13].…”

Section: Introductionmentioning

confidence: 99%

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RNase Y-mediated regulation of the streptococcal pyrogenic exotoxin B

et al. 2018

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Endoribonuclease Y (RNase Y) is a crucial regulator of virulence in Gram-positive bacteria. In the human pathogen Streptococcus pyogenes, RNase Y is required for the expression of the major secreted virulence factor streptococcal pyrogenic exotoxin B (SpeB), but the mechanism involved in this regulation remains elusive. Here, we demonstrate that the 5′ untranslated region of speB mRNA is processed by several RNases including RNase Y. In particular, we identify two RNase Y cleavage sites located downstream of a guanosine (G) residue. To assess whether this nucleotide is required for RNase Y activity in vivo, we mutated it and demonstrate that the presence of this G residue is essential for the processing of the speB mRNA 5′ UTR by RNase Y. Although RNase Y directly targets and processes speB, we show that RNase Y-mediated regulation of speB expression occurs primarily at the transcriptional level and independently of the processing in the speB mRNA 5′ UTR. To conclude, we demonstrate for the first time that RNase Y processing of an mRNA target requires the presence of a G. We also provide new insights on the speB 5′ UTR and on the role of RNase Y in speB regulation.

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Section: Resultssupporting

confidence: 66%

Section: Discussioncontrasting

confidence: 58%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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RNase Y-mediated regulation of the streptococcal pyrogenic exotoxin B

et al. 2018

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“…31 RNase J belongs to the same family of enzymes (the β-CASP subgroup of the Zn-dependent metallo-β-lactamases) as the eukaryotic cleavage and polyadenylation factor CPSF-73. Intriguingly, this protein also forms a complex with a paralagous but catalytically inactive enzyme, CPSF-100, and is also thought to have 10,34 Depletion of this membrane-bound essential protein causes an even greater defect (>two-fold) in global mRNA decay rates than depletion of RNase J1/J2. Like RNase E, the endonucleolytic activity of RNase Y is dependent on the 5'-phosphorylation status of the RNA substrate.…”

Section: Role Of Rnase J In Other Organismsmentioning

confidence: 99%

What is the role of RNase J in mRNA turnover?

Condon¹

2010

RNA Biology

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T he discovery of the paralogous ribonucleases J1 and J2 has been a major advance in the study of RNA maturation and decay in Bacillus subtilis and related organisms. RNase J1 was the first bacterial enzyme shown to possess 5'-to-3' exoribonuclease activity, reversing a dogma that suggested this type of activity was unique to eukaryotic mRNA decay. RNase J1 and J2 form a complex that also has endonuclease activity and these enzymes have been shown to play a key role in the turnover and maturation of many RNAs in B. subtilis. Here, I describe recent progress in our understanding of the role of these enzymes in RNA metabolism in this organism and argue that the 5'-to-3' exoribonuclease activity may be the more important of the complex's two modes of action.

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m RNA Stability

Kaberdin

Bläsi

2014

Encyclopedia of Life Sciences

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The steady‐state level of a messenger ribonucleic acid (mRNA) is determined by both its rate of synthesis and degradation. The degradation of mRNA is an important tool employed by cells to control gene expression and to adjust the level of protein synthesis in response to physiological needs or environmental signals. The degradation of mRNA in all organisms is mastered by a rather restricted number of enzymes with major (endo‐ and exoribonucleases) and ancillary (e.g. RNA helicases) functions. Some of these enzymes are phylogenetically conserved across the three domains of life – bacteria, archaea and eukarya. Moreover, the main components of the RNA decay machinery can associate with each other to form multienzyme complexes, which enable to coordinate and control mRNA decay in vivo . This review provides a brief overview on the major factors and mechanisms involved in bacterial and eukaryal mRNA degradation. Key Concepts: The stability of individual mRNAs varies and is dependent on intrinsic properties (i.e. specific structure and sequence) of transcripts. The enzymes and factors involved in mRNA decay in prokaryotes and eukaryotes can associate with each other to form multienzyme complexes such as degradosomes or exosomes Mechanisms of mRNA decay in pro‐ and eukaryotes share many common steps. Pro‐ and eukaryotic cells use specific mechanisms to eliminate defective mRNAs. Numerous noncoding RNAs control mRNA decay in pro‐ and eukaryotes.

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RNase Y, a novel endoribonuclease, initiates riboswitch turnover in Bacillus subtilis

Cited by 219 publications

References 39 publications

RNase Y-mediated regulation of the streptococcal pyrogenic exotoxin B

RNase Y-mediated regulation of the streptococcal pyrogenic exotoxin B

What is the role of RNase J in mRNA turnover?

m RNA Stability

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