Control of Expression of the RNases J1 and J2 in Bacillus subtilis

In Bacillus subtilis, the dual activity 5′ exo- and endoribonucleases J1 and J2 are important players in mRNA and stable RNA maturation and degradation. Recent work has improved our understanding of their structure and mechanism of action and identified numerous RNA substrates. However, almost nothi...

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Bibliographic Details
Published in:Journal of Bacteriology 2014-01, Vol.196 (2), p.318-324
Main Authors: Jamalli, Ailar, Hébert, Agnès, Zig, Léna, Putzer, Harald
Format: Article
Language:English
Subjects:
Bacillus subtilis
Bacillus subtilis - enzymology
Bacillus subtilis - genetics
Bacteriology
Biosynthesis
endoribonucleases
Enzymes
Gene expression
Gene Expression Regulation, Bacterial
Genetics
Gram-positive bacteria
mechanism of action
messenger RNA
operon
Promoter Regions, Genetic
Protein Biosynthesis
Protein Multimerization
Ribonucleases - biosynthesis
Ribonucleic acid
RNA
transcription (genetics)
Transcription, Genetic
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Summary:In Bacillus subtilis, the dual activity 5′ exo- and endoribonucleases J1 and J2 are important players in mRNA and stable RNA maturation and degradation. Recent work has improved our understanding of their structure and mechanism of action and identified numerous RNA substrates. However, almost nothing is known about the expression of these enzymes. Here, we have identified the transcriptional and translational signals that control the expression of the rnjA (RNase J1) and rnjB (RNase J2) genes. While the rnjB gene is transcribed constitutively from a sigma A promoter, optimal expression of RNase J1 requires cotranscription and cotranslation with the upstream ykzG gene, encoding a protein of unknown function. In the absence of coupled translation, RNase J1 expression is decreased more than 5-fold. Transcription of the ykzG operon initiates at a sigma A promoter with a noncanonical −35 box that is required for optimal transcription. Biosynthesis of RNase J1 is autocontrolled within a small range (1.4-fold) and also slightly stimulated (1.4-fold) in the absence of RNase J2. These controls are weak but might be useful to maintain the overall RNase J level and possibly also equimolar amounts of the two nucleases in the cell that primarily act as a heterodimer in vivo.
ISSN:0021-9193
1098-5530
1067-8832
DOI:10.1128/jb.01053-13