title: Staphylococcus aureus RNAIII and the endoribonuclease III coordinately regulate spa gene expression.
abstract: Staphylococcus aureus RNAIII is one of the largest regulatory RNAs, which controls several virulence genes encoding exoproteins and cell-wall-associated proteins. One of the RNAIII effects is the repression of spa gene (coding for the surface protein A) expression. Here, we show that spa repression occurs not only at the transcriptional level but also by RNAIII-mediated inhibition of translation and degradation of the stable spa mRNA by the double-strand-specific endoribonuclease III (RNase III). The 3' end domain of RNAIII, partially complementary to the 5' part of spa mRNA, efficiently anneals to spa mRNA through an initial loop-loop interaction. Although this annealing is sufficient to inhibit in vitro the formation of the translation initiation complex, the coordinated action of RNase III is essential in vivo to degrade the mRNA and irreversibly arrest translation. Our results further suggest that RNase III is recruited for targeting the paired RNAs. These findings add further complexity to the expression of the S. aureus virulon.
authors.affiliation: UPR 9002 du CNRS, Institut de Biologie Moléculaire et Cellulaire, Strasbourg Cedex, France.
authors.forename: Eric
authors.initials: E
authors.lastname: Huntzinger
authors.forename: Sandrine
authors.initials: S
authors.lastname: Boisset
authors.forename: Cosmin
authors.initials: C
authors.lastname: Saveanu
authors.forename: Yvonne
authors.initials: Y
authors.lastname: Benito
authors.forename: Thomas
authors.initials: T
authors.lastname: Geissmann
authors.forename: Abdelkader
authors.initials: A
authors.lastname: Namane
authors.forename: Gérard
authors.initials: G
authors.lastname: Lina
authors.forename: Jerome
authors.initials: J
authors.lastname: Etienne
authors.forename: Bernard
authors.initials: B
authors.lastname: Ehresmann
authors.forename: Chantal
authors.initials: C
authors.lastname: Ehresmann
authors.forename: Alain
authors.initials: A
authors.lastname: Jacquier
authors.forename: François
authors.initials: F
authors.lastname: Vandenesch
authors.forename: Pascale
authors.initials: P
authors.lastname: Romby
mesh_terms: D000942:Antigens, Bacterial / Q000235:genetics* / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism; D001483:Base Sequence; D001665:Binding Sites; D015964:Gene Expression Regulation, Bacterial; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D014176:Protein Biosynthesis; D020871:RNA Stability; D016372:RNA, Antisense / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D012329:RNA, Bacterial / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D043244:Ribonuclease III / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism; D013205:Staphylococcal Protein A / Q000235:genetics / Q000378:metabolism; D013211:Staphylococcus aureus / Q000201:enzymology* / Q000235:genetics*; D014158:Transcription, Genetic / Q000235:genetics
chemical_list: D000942:Antigens, Bacterial; D001426:Bacterial Proteins; D016372:RNA, Antisense; D012329:RNA, Bacterial; D012333:RNA, Messenger; C096035:RNAIII, Staphylococcus aureus; D013205:Staphylococcal Protein A; C119204:streptococcal protective antigen; D043244:Ribonuclease III