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Microbiology and Molecular Biology Reviews, June 2003, p. 157-174, Vol. 67, No. 2
1092-2172/03/$08.00+0     DOI: 10.1128/MMBR.67.2.157-174.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

RNA Processing and Degradation in Bacillus subtilis

Ciarán Condon*

UPR 9073, Institut de Biologie Physico-Chimique, 75005 Paris, France

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.

* Mailing address: UPR 9073, Institut de Biologie Physico-Chi-mique, 13 rue Pierre et Marie Curie, 75005 Paris, France. Phone: (33)-1-58 41 51 23. Fax: (33)-1-58 41 50 25. E-mail: condon{at}ibpc.fr.

Microbiology and Molecular Biology Reviews, June 2003, p. 157-174, Vol. 67, No. 2
1092-2172/03/$08.00+0     DOI: 10.1128/MMBR.67.2.157-174.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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