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TitleAn RNA degradation machine sculpted by Ro autoantigen and noncoding RNA.
Journal, issue, pagesCell, Vol. 153, Issue 1, Page 166-177, Year 2013
Publish dateMar 28, 2013
AuthorsXinguo Chen / David W Taylor / Casey C Fowler / Jorge E Galan / Hong-Wei Wang / Sandra L Wolin /
PubMed AbstractMany bacteria contain an ortholog of the Ro autoantigen, a ring-shaped protein that binds noncoding RNAs (ncRNAs) called Y RNAs. In the only studied bacterium, Deinococcus radiodurans, the Ro ...Many bacteria contain an ortholog of the Ro autoantigen, a ring-shaped protein that binds noncoding RNAs (ncRNAs) called Y RNAs. In the only studied bacterium, Deinococcus radiodurans, the Ro ortholog Rsr functions in heat-stress-induced ribosomal RNA (rRNA) maturation and starvation-induced rRNA decay. However, the mechanism by which this conserved protein and its associated ncRNAs act has been obscure. We report that Rsr and the exoribonuclease polynucleotide phosphorylase (PNPase) form an RNA degradation machine that is scaffolded by Y RNA. Single-particle electron microscopy, followed by docking of atomic models into the reconstruction, suggests that Rsr channels single-stranded RNA into the PNPase cavity. Biochemical assays reveal that Rsr and Y RNA adapt PNPase for effective degradation of structured RNAs. A Ro ortholog and ncRNA also associate with PNPase in Salmonella Typhimurium. Our studies identify another ribonucleoprotein machine and demonstrate that ncRNA, by tethering a protein cofactor, can alter the substrate specificity of an enzyme.
External linksCell / PubMed:23540697 / PubMed Central
MethodsEM (single particle)
Resolution25.0 Å
Structure data

EMDB-5389:
An RNA Degradation Machine Sculpted by Ro Autoantigen and Noncoding RNA
Method: EM (single particle) / Resolution: 25.0 Å

Source
  • Deinococcus radiodurans (radioresistant)

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