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Degradation of nanoRNA is performed by multiple redundant RNases in Bacillus subtilis

Authors :
Ciarán Condon
Undine Mechold
Antoine Danchin
Vasily Ogryzko
Ming Fang
Wencke-Maria Zeisberg
Génétique des Génomes Bactériens
Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS)
Institut de biologie physico-chimique (IBPC (FR_550))
Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)
Interactions moléculaires et cancer (IMC (UMR 8126))
Signalisation, noyaux et innovations en cancérologie (UMR8126)
Université Paris-Sud - Paris 11 (UP11)-Institut Gustave Roussy (IGR)-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Sud - Paris 11 (UP11)-Institut Gustave Roussy (IGR)-Centre National de la Recherche Scientifique (CNRS)
European Union Network of Excellence BioSapiens[LSHG CT-2003-503265 to A.D.]
the French ResearchAgency (Agence nationale de la recherche) [BLAN06-3_135068 toC.C.]
La Ligue Contre le Cancer[9ADO1217/1B1-BIOCE to V.O.]
Institut national duCancer [247343/1B1-BIOCE to V.O.]. Funding for openaccess charge: Institut Pasteur.
Centre National de la Recherche Scientifique (CNRS)-Institut Pasteur [Paris]
Centre National de la Recherche Scientifique (CNRS)
Source :
Nucleic Acids Research, Nucleic Acids Research, 2009, 37 (15), pp.5114-25. ⟨10.1093/nar/gkp527⟩, Nucleic Acids Research, Oxford University Press, 2009, 37 (15), pp.5114-25. ⟨10.1093/nar/gkp527⟩
Publication Year :
2009
Publisher :
HAL CCSD, 2009.

Abstract

International audience; 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.

Details

Language :
English
ISSN :
03051048 and 13624962
Database :
OpenAIRE
Journal :
Nucleic Acids Research, Nucleic Acids Research, 2009, 37 (15), pp.5114-25. ⟨10.1093/nar/gkp527⟩, Nucleic Acids Research, Oxford University Press, 2009, 37 (15), pp.5114-25. ⟨10.1093/nar/gkp527⟩
Accession number :
edsair.doi.dedup.....e9d66f636e68fc51da61182aeb83cf59
Full Text :
https://doi.org/10.1093/nar/gkp527⟩