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Science 6 April 2007:
Vol. 316. no. 5821, pp. 115 - 120
DOI: 10.1126/science.1137924
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Reports

Binding of the Human Prp31 Nop Domain to a Composite RNA-Protein Platform in U4 snRNP

Sunbin Liu,1* Ping Li,1,2* Olexandr Dybkov,1 Stephanie Nottrott,1 Klaus Hartmuth,1 Reinhard Lührmann,1{dagger} Teresa Carlomagno,2{dagger} Markus C. Wahl3{dagger}

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.

1 Abteilung Zelluläre Biochemie, Max-Planck-Institut für Biophysikalische Chemie, Am Faßberg 11, D-37077 Göttingen, Germany.
2 AG Flüssig-NMR Spektroskopie, Max-Planck-Institut für Biophysikalische Chemie, Am Faßberg 11, D-37077 Göttingen, Germany.
3 AG Makromolekulare Röntgenkristallographie, Max-Planck-Institut für Biophysikalische Chemie, Am Faßberg 11, D-37077 Göttingen, Germany.

* These authors contributed equally to this work.

{dagger} To whom correspondence should be addressed. E-mail: Reinhard.Luehrmann{at}mpi-bpc.mpg.de (R.L.); taco{at}nmr.mpibpc.mpg.de (T.C.); mwahl{at}gwdg.de (M.C.W.)

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