An RNA degradation machine sculpted by Ro autoantigen and noncoding RNA.
An RNA degradation machine sculpted by Ro autoantigen and noncoding RNA.
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DOI:
10.1016/j.cell.2013.02.037
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发表时间:
2013-03-28
期刊:
影响因子:
64.5
通讯作者:
Wolin SL
中科院分区:
文献类型:
--
作者:
Chen X;Taylor DW;Fowler CC;Galan JE;Wang HW;Wolin SL
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 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 a new ribonucleoprotein machine and demonstrate that ncRNA, by tethering a protein cofactor, can alter the substrate specificity of an enzyme.
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