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An ortholog of the Ro autoantigen functions in 23S rRNA maturation in D. radiodurans

¹ Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06536, USA; ² Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, Connecticut 06536, USA; ³ Stowers Institute for Medical Research, Kansas City, Missouri 64110, USA

In both animal cells and the eubacterium Deinococcus radiodurans, the Ro autoantigen, a ring-shaped RNA-binding protein, associates with small RNAs called Y RNAs. In vertebrates, Ro also binds the 3' ends of misfolded RNAs and is proposed to function in quality control. However, little is known about the function of Ro and the Y RNAs in vivo. Here, we report that the D. radiodurans ortholog Rsr (Ro sixty related) functions with exoribonucleases in 23S rRNA maturation. During normal growth, 23S rRNA maturation is inefficient, resulting in accumulation of precursors containing 5' and 3' extensions. During growth at elevated temperature, maturation is efficient and requires Rsr and the exoribonucleases RNase PH and RNase II. Consistent with the hypothesis that Y RNAs inhibit Ro activity, maturation is efficient at all temperatures in cells lacking the Y RNA. In the absence of Rsr, 23S rRNA maturation halts at positions of potential secondary structure. As Rsr exhibits genetic and biochemical interactions with the exoribonuclease polynucleotide phosphorylase, Rsr likely functions in an additional process with this nuclease. We propose that Rsr functions as a processivity factor to assist RNA maturation by exoribonucleases. This is the first demonstration of a role for Ro and a Y RNA in vivo.

[Keywords: Ro ribonucleoprotein; Y RNA; exoribonucleases; rRNA processing; D. radiodurans]

Received March 5, 2007; revised version accepted April 3, 2007.

E-MAIL sandra.wolin{at}yale.edu; FAX (203) 737-1761.

Article published online ahead of print. Article and publication date are online at http://www.genesdev.org/cgi/doi/10.1101/gad.1548207

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