Functional analysis of 11 putative essential genes in Bacillus subtilis

Hunt, Alison; Rawlins, Joy P.; Thomaides, Helena B.; Errington, Jeff

doi:10.1099/mic.0.29152-0

Cited by 110 publications

(130 citation statements)

References 37 publications

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“…3 This presumably accounts for the enzyme's association with the ribosome. 4,5 In parallel, the Putzer laboratory went searching for an enzyme that cleaved the thrS leader at another site in vitro, about 180 nts upstream of the site cleaved by the B. subtilis RNase E-like enzyme. These two sites are referred to as site 1 and site 2 in the order of their occurrence in the thrS transcript.…”

Section: Introductionmentioning

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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Section: Introductionmentioning

confidence: 99%

What is the role of RNase J in mRNA turnover?

Condon¹

2010

RNA Biology

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“…The GTPase activity of CpgA is thus probably important for efficient ribosome maturation and consequently for bacterial growth. In line with this idea, both cpgA from B. subtilis and rsgA from E. coli were first described as essential genes (33), even though their essentiality has been controversial and, in both bacteria, knock-out viable mutants were eventually obtained (12,24,34). We show that CpgA is phosphorylated by PrkC on Thr-166 and that this phosphorylation likely governs the cellular function of CpgA.…”

Section: Discussionmentioning

confidence: 67%

Phosphorylation of CpgA Protein Enhances Both Its GTPase Activity and Its Affinity for Ribosome and Is Crucial for Bacillus subtilis Growth and Morphology

Pompeo¹,

Freton²,

Wicker‐Planquart³

et al. 2012

Journal of Biological Chemistry

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Background:CpgA is an essential GTPase phosphorylated in vitro by the Ser/Thr kinase PrkC. Results: CpgA is phosphorylated on Thr-166, and phosphomimetic or phosphoablative replacements of this residue in CpgA modify its GTPase activity. Conclusion: Phosphorylation of CpgA is probably a key regulatory feature of B. subtilis physiology. Significance: The regulation of CpgA via phosphorylation may be needed in sporulating B. subtilis cells.

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“…Mutations in the highly conserved HD motif strongly reduce the endonucleolytic activity of RNase Y, indicating that the catalytic activity resides within the HD domain (20). This also suggests that it is the impaired ribonucleolytic activity that causes previously observed defects of an RNase Y mutation (formerly ymdA) in cell and chromosome morphology (81).…”

Section: Protein Structure and Catalytic Mechanismmentioning

confidence: 75%

“…RNase E and other degradosome components are associated with the inner surface of the cell (110), interact with the bacterial cytoskeleton (111,112) and the inner membrane (113). RNase Y has a transmembrane domain at its N-terminus and has been localized at the membrane in vivo (81). This sublocalization might have important consequences for the fate of an mRNA.…”

Section: Multiprotein Complexes and Cellular Localizationmentioning

confidence: 99%

mRNA degradation and maturation in prokaryotes: the global players

Laalami

Putzer

2011

BioMolecular Concepts

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The degradation of messenger RNA is of universal importance for controlling gene expression. It directly affects protein synthesis by modulating the amount of mRNA available for translation. Regulation of mRNA decay provides an efficient means to produce just the proteins needed and to rapidly alter patterns of protein synthesis. In bacteria, the half-lives of individual mRNAs can differ by as much as two orders of magnitude, ranging from seconds to an hour. Most of what we know today about the diverse mechanisms of mRNA decay and maturation in prokaryotes comes from studies of the two model organisms Escherichia coli and Bacillus subtilis. Their evolutionary distance provided a large picture of potential pathways and enzymes involved in mRNA turnover. Among them are three ribonucleases, two of which have been discovered only recently, which have a truly general role in the initiating events of mRNA degradation: RNase E, RNase J and RNase Y. Their enzymatic characteristics probably determine the strategies of mRNA metabolism in the organism in which they are present. These ribonucleases are coded, alone or in various combinations, in all prokaryotic genomes, thus reflecting how mRNA turnover has been adapted to different ecological niches throughout evolution.

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Functional analysis of 11 putative essential genes in Bacillus subtilis

Cited by 110 publications

References 37 publications

What is the role of RNase J in mRNA turnover?

What is the role of RNase J in mRNA turnover?

Phosphorylation of CpgA Protein Enhances Both Its GTPase Activity and Its Affinity for Ribosome and Is Crucial for Bacillus subtilis Growth and Morphology

mRNA degradation and maturation in prokaryotes: the global players

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