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A common core RNP structure shared between the small nucleolar box C/D RNPs and the spliceosomal U4 snRNP

Lookup NU author(s): Dr Nick Watkins

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Abstract

The box C/D snoRNAs function in directing 2'-O-methylation and/or as chaperones in the processing of ribosomal RNA. We show here that Snu13p (15.5 kD in human), a component of the U4/U6.U5 tri-snRNP, is also associated with the box C/D snoRNAs. Indeed, genetic depletion of Snu13p in yeast leads to a major defect in RNA metabolism. The box C/D motif can be folded into a stem-internal loop-stem structure, almost identical to the 15.5 kD binding site in the U4 snRNA. Consistent with this, the box C/D motif binds Snu13p/ 15.5 kD in vitro. The similarities in structure and function observed between the U4 snRNP (chaperone for U6) and the box C/D snoRNPs raises the interesting possibility that these particles may have evolved from a common ancestral RNP.

Publication metadata

Author(s): Watkins NJ, Segault V, Charpentier B, Nottrott S, Fabrizio P, Bachi A, Wilm M, Rosbash M, Branlant C, Lührmann R

Publication type: Article

Publication status: Published

Journal: Cell

Year: 2000

Volume: 103

Issue: 3

Pages: 457-466

Publisher: Elsevier

URL: http://dx.doi.org/ 10.1016/S0092-8674(00)00137-9

DOI: 10.1016/S0092-8674(00)00137-9

PubMed id: 11081632

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