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Bacillus subtilis mRNA decay: new parts in the toolkit

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Abstract Representatives of two new ribonuclease families have recently been discovered in the gram‐positive model organism, Bacillus subtilis. The RNase J family founding members, RNase J1 and RNase J2, are highly homologous but show differential activities. Although both are broad‐specificity endonucleases, only the essential RNase J1 is a 5′ → 3′ exonuclease—a type of ribonuclease activity that was previously thought not to exist in bacteria. Current data suggest that RNase J1 is highly involved in the turnover of mRNA decay intermediates and may also be involved in the initiation of mRNA decay. A second family of ribonucleases is represented by RNase Y, an endonuclease that exerts a large effect on global mRNA half‐life. The presence of these ribonucleases in B. subtilis predicts significant differences from the well‐established model of mRNA decay in Escherichia coli. WIREs RNA 2011 2 387–394 DOI: 10.1002/wrna.66 This article is categorized under: RNA Turnover and Surveillance > Regulation of RNA Stability RNA Turnover and Surveillance > Turnover/Surveillance Mechanisms

Ribbon diagram of domain structure of RNase J from Thermus thermophilus. The deep cleft between the β‐CASP and β‐lactamase is occupied by the 5′ monophosphorylated end of an mRNA molecule. Dark blue spheres represent zinc ions at the catalytic site. Location of two‐residue mutation (D78K;H79A) between β‐strand 5 and α‐helix 2, which inactivates both ribonuclease activities,11 is indicated.

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Three modes of RNase J1 involvement in mRNA decay. RNase J1 is shown as a combination 5′ exonuclease (Pac‐Man) and endonuclease (scissors), in a complex with RNase J2 (behind). (a) Attack of mRNA from the native 5′ end after removal of 5′ pyrophosphate. (b) Attack of mRNA downstream fragment following internal cleavage by RNase Y. (c) Successive endonucleolytic and 5′ exonucleolytic attack without release of substrate.

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Domain structure of RNase Y. Amino‐acid residue numbers mark approximate boundaries of predicted domains.

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RNA Turnover and Surveillance > Turnover/Surveillance Mechanisms
RNA Turnover and Surveillance > Regulation of RNA Stability

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