Degradation of nanoRNA is performed by multiple redundant RNases in Bacillus subtilis
Open Access
- 24 June 2009
- journal article
- research article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 37 (15) , 5114-5125
Abstract
Escherichia coli possesses only one essential oligoribonuclease (Orn), an enzyme that can degrade oligoribonucleotides of five residues and shorter in length (nanoRNA). Firmicutes including Bacillus subtilis do not have an Orn homolog. We had previously identified YtqI (NrnA) as functional analog of Orn in B. subtilis . Screening a genomic library from B. subtilis for genes that can complement a conditional orn mutant, we identify here YngD (NrnB) as a second nanoRNase in B. subtilis . Like NrnA, NrnB is a member of the DHH/DHHA1 protein family of phosphoesterases. NrnB degrades nanoRNA 5-mers in vitro similarily to Orn. Low expression levels of NrnB are sufficient for orn complementation. YhaM, a known RNase present in B. subtilis , degrades nanoRNA efficiently in vitro but requires high levels of expression for only partial complementation of the orn – strain. A triple mutant ( nrnA– , nrnB– , yhaM– ) in B. subtilis is viable and shows almost no impairment in growth. Lastly, RNase J1 seems also to have some 5′-to-3′ exoribonuclease activity on nanoRNA and thus can potentially finish degradation of RNA. We conclude that, unlike in E. coli , degradation of nanoRNA is performed in a redundant fashion in B. subtilis .Keywords
This publication has 33 references indexed in Scilit:
- Role of Bacillus subtilis RNase J1 Endonuclease and 5′-Exonuclease Activities in trp Leader RNA TurnoverJournal of Biological Chemistry, 2008
- YtqI from Bacillus subtilis has both oligoribonuclease and pAp-phosphatase activityNucleic Acids Research, 2007
- The role of the S1 domain in exoribonucleolytic activity: Substrate specificity and multimerizationRNA, 2007
- CDD: a conserved domain database for interactive domain family analysisNucleic Acids Research, 2006
- Substrate Recognition and Catalysis by the Exoribonuclease RNase RJournal of Biological Chemistry, 2006
- Characterization of the Functional Domains of Escherichia coli RNase IIJournal of Molecular Biology, 2006
- Oligoribonuclease is a common downstream target of lithium-induced pAp accumulation in Escherichia coli and human cellsNucleic Acids Research, 2006
- Identification of sporulation genes by genome-wide analysis of the σ E regulon of Bacillus subtilisMicrobiology, 2003
- Bacillus subtilisYhaM, a Member of a New Family of 3′-to-5′ Exonucleases in Gram-Positive BacteriaJournal of Bacteriology, 2002
- PcrA is an essential DNA helicase of Bacillus subtilis fulfilling functions both in repair and rolling‐circle replicationMolecular Microbiology, 1998