Binding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNP
S Liu, P Li, O Dybkov, S Nottrott, K Hartmuth… - Science, 2007 - science.org
S Liu, P Li, O Dybkov, S Nottrott, K Hartmuth, R Lührmann, T Carlomagno, MC Wahl
Science, 2007•science.orgAlthough 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 15.5 K protein and U4 or U4atac small nuclear RNA (snRNA),
whereas Nop56/58 associate with 15.5 K–box C/D small nucleolar RNA complexes. We
present structural and biochemical analyses of hPrp31-15.5 K-U4 snRNA complexes that
show how the conserved Nop domain in hPrp31 maintains high RNP binding selectivity …
(Nop56/58) proteins recognize different ribonucleoprotein (RNP) particles. hPrp31 interacts
with complexes containing the 15.5 K protein and U4 or U4atac small nuclear RNA (snRNA),
whereas Nop56/58 associate with 15.5 K–box C/D small nucleolar RNA complexes. We
present structural and biochemical analyses of hPrp31-15.5 K-U4 snRNA complexes that
show how the conserved Nop domain in hPrp31 maintains high RNP binding selectivity …
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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