title: Both exo- and endo-nucleolytic activities of RNase J1 from Staphylococcus aureus are manganese dependent and active on triphosphorylated 5'-ends.
abstract: RNA decay and RNA maturation are important steps in the regulation of bacterial gene expression. RNase J, which is present in about half of bacterial species, has been shown to possess both endo- and 5' to 3' exo-ribonuclease activities. The exonucleolytic activity is clearly involved in the degradation of mRNA and in the maturation of at least the 5' end of 16S rRNA in the 2 Firmicutes Staphylococcus aureus and Bacillus subtilis. The endoribonuclease activity of RNase J from several species has been shown to be weak in vitro and 3-D structural data of different RNase J orthologs have not provided a clear explanation for the molecular basis of this activity. Here, we show that S. aureus RNase J1 is a manganese dependent homodimeric enzyme with strong 5' to 3' exo-ribonuclease as well as endo-ribonuclease activity. In addition, we demonstrated that SauJ1 can efficiently degrade 5' triphosphorylated RNA. Our results highlight RNase J1 as an important player in RNA turnover in S. aureus.
authors.affiliation: a Department of Microbiology and Molecular Medicine , Medical Faculty, University of Geneva , Geneva , Switzerland.
authors.forename: Stéphane
authors.initials: S
authors.lastname: Hausmann
authors.affiliation: a Department of Microbiology and Molecular Medicine , Medical Faculty, University of Geneva , Geneva , Switzerland.
authors.forename: Vanessa Andrade
authors.initials: VA
authors.lastname: Guimarães
authors.affiliation: a Department of Microbiology and Molecular Medicine , Medical Faculty, University of Geneva , Geneva , Switzerland.
authors.forename: Dominique
authors.initials: D
authors.lastname: Garcin
authors.affiliation: a Department of Microbiology and Molecular Medicine , Medical Faculty, University of Geneva , Geneva , Switzerland.
authors.forename: Natalia
authors.initials: N
authors.lastname: Baumann
authors.affiliation: a Department of Microbiology and Molecular Medicine , Medical Faculty, University of Geneva , Geneva , Switzerland.
authors.forename: Patrick
authors.initials: P
authors.lastname: Linder
authors.affiliation: a Department of Microbiology and Molecular Medicine , Medical Faculty, University of Geneva , Geneva , Switzerland.|b Laboratoire de Microbiologie et de Génétique Moléculaires, Centre de Biologie Intégrative, Université de Toulouse III Toulouse , France.
authors.forename: Peter
authors.initials: P
authors.lastname: Redder
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D003001:Cloning, Molecular; D015964:Gene Expression Regulation, Bacterial; D008345:Manganese / Q000378:metabolism*; D010766:Phosphorylation; D020836:Protein Structure, Quaternary; D012260:Ribonucleases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D013211:Staphylococcus aureus / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development
chemical_list: D001426:Bacterial Proteins; D008345:Manganese; D012260:Ribonucleases
keywords: Endoribonuclease; RNase J1; S. aureus; exoribonuclease; manganese; triphosphorylated RNA