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. 2007 Apr 6;316(5821):115-20.
doi: 10.1126/science.1137924.

Binding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNP

Sunbin Liu  1 , Ping Li, Olexandr Dybkov, Stephanie Nottrott, Klaus Hartmuth, Reinhard Lührmann, Teresa Carlomagno, Markus C Wahl
Affiliations

Binding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNP

Sunbin Liu et al. Science. .

Abstract

Although highly homologous, the spliceosomal hPrp31 and the nucleolar Nop56 and Nop58 (Nop56/58) proteins recognize different ribonucleoprotein (RNP) particles. hPrp31 interacts with complexes containing the 15.5K protein and U4 or U4atac small nuclear RNA (snRNA), whereas Nop56/58 associate with 15.5K-box C/D small nucleolar RNA complexes. We present structural and biochemical analyses of hPrp31-15.5K-U4 snRNA complexes that show how the conserved Nop domain in hPrp31 maintains high RNP binding selectivity despite relaxed RNA sequence requirements. The Nop domain is a genuine RNP binding module, exhibiting RNA and protein binding surfaces. Yeast two-hybrid analyses suggest a link between retinitis pigmentosa and an aberrant hPrp31-hPrp6 interaction that blocks U4/U6-U5 tri-snRNP formation.

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