Journal
NUCLEIC ACIDS RESEARCH
Volume 45, Issue 6, Pages 3559-3567Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkw1323
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Funding
- National Natural Science Foundation of China [31430024, 91540201, 31325007]
- Strategic Priority Research Program of the Chinese Academy of Sciences [XDB08010203]
- Beijing Municipal Government
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The assembly of eukaryotic ribosomes requires numerous factors that transiently associate with evolving pre-ribosomal particles. The Pumilio repeatcontaining protein Nop9 briefly associates with the 90S pre-ribosome during its co-transcriptional assembly. Here, we show that Nop9 specifically binds an 11-nucleotide sequence of 18S rRNA that forms the 3' side of the central pseudoknot and helix 28 in the mature subunit. Crystal structures of Nop9 in the free and RNA-bound states reveal a new type of Pumilio repeat proteinwith a distinct structure, target sequence and RNA-binding mode. Nop9 contains 10 Pumilio repeats arranged into a U-shaped scaffold. The target RNA is recognized by two stretches of repeats in a bipartite manner, and three central bases are unrecognized as a result of the degeneracy of repeats 6 and 7. Our data suggest that Nop9 regulates the folding of 18S rRNA at early assembly stages of 90S.
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