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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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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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S. Boulon, N. Marmier-Gourrier, B. Pradet-Balade, L. Wurth, C. Verheggen, B. E. Jady, B. Rothe, C. Pescia, M.-C. Robert, T. Kiss, et al. (2008)
J. Cell Biol. 180, 579-595
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Dynamic Interactions of Ntr1-Ntr2 with Prp43 and with U5 Govern the Recruitment of Prp43 To Mediate Spliceosome Disassembly.
R.-T. Tsai, C.-K. Tseng, P.-J. Lee, H.-C. Chen, R.-H. Fu, K.-j. Chang, F.-L. Yeh, and S.-C. Cheng (2007)
Mol. Cell. Biol. 27, 8027-8037
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Improved identification of enriched peptide RNA cross-links from ribonucleoprotein particles (RNPs) by mass spectrometry.
E. Kuhn-Holsken, O. Dybkov, B. Sander, R. Luhrmann, and H. Urlaub (2007)
Nucleic Acids Res. 35, e95
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Science. ISSN 0036-8075 (print), 1095-9203 (online)