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RESEARCH PAPER
Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602, USA
In eukaryotes and archaea, uridines in various RNAs are converted to pseudouridines by RNA-guided RNA modification complexes termed H/ACA RNPs. Guide RNAs within the complexes base-pair with target RNAs to direct modification of specific ribonucleotides. Cbf5, a protein component of the complex, likely catalyzes the modification. However, little is known about the organization of H/ACA RNPs and the roles of the multiple proteins thought to comprise the complexes. We have reconstituted functional archaeal H/ACA RNPs from recombinant components, defined the components necessary and sufficient for function, and determined the direct RNA–protein and protein–protein interactions that occur between the components. The results provide substantial insight into the functional organization of this RNP. The functional complex requires a guide RNA and each of four proteins: Cbf5, Gar1, L7Ae, and Nop10. Two proteins interact directly with the guide RNA: L7Ae and Cbf5. L7Ae does not interact with other H/ACA RNP proteins in the absence of the RNA. We have defined two novel functions for Cbf5. Cbf5 is the protein that specifically recognizes and binds H/ACA guide RNAs. In addition, Cbf5 recruits the two other essential proteins, Gar1 and Nop10, to the pseudouridylation guide complex.
[Keywords: Noncoding RNA; RNA modification; RNA–protein complex; archaea; pseudouridylation]
Received February 24, 2005; revised version accepted April 1, 2005.
Article published online ahead of print. Article and publication date are at http://www.genesdev.org/cgi/doi/10.1101/gad.1309605.
1 These authors contributed equally to this work.
2 E-MAIL rterns{at}bmb.uga.edu; FAX (706) 542-1752.
3 E-MAIL mterns{at}bmb.uga.edu; FAX (706) 542-1752.
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