Search Organism: All OrganismsArabidopsis thalianaBacillus subtilis 168Bos taurusCaenorhabditis elegansCanis familiarisDanio rerioDrosophila melanogasterEquus caballusEscherichia coli K12Gallus gallusHomo sapiensMacaca mulattaMus musculusNematostella vectensisOryza sativaPan troglodytesRattus norvegicusSaccharomyces cerevisiaeSchizosaccharomyces pombeStrongylocentrotus purpuratusTakifugu rubripesXenopus laevis home help / support contribute downloads mirrors about us Mol. Cell. Biol. Nov (2005); 25(21):9269-82 The splicing ATPase prp43p is a component of multiple preribosomal particles- Lebaron S, Froment C, Fromont-Racine M, Rain JC, Monsarrat B, Caizergues-Ferrer M, Henry Y Laboratoire de Biologie Moleculaire Eucaryote, UMR5099 CNRS-Universite Paul Sabatier, IFR109, 118 route de Narbonne, 31062 Toulouse cedex 09, France- Abstract: Prp43p is a putative helicase of the DEAH family which is required for the release of the lariat intron from the spliceosome- Prp43p could also play a role in ribosome synthesis, since it accumulates in the nucleolus- Consistent with this hypothesis, we find that depletion of Prp43p leads to accumulation of 35S pre-rRNA and strongly reduces levels of all downstream pre-rRNA processing intermediates- As a result, the steady-state levels of mature rRNAs are greatly diminished following Prp43p depletion- We present data arguing that such effects are unlikely to be solely due to splicing defects- Moreover, we demonstrate by a combination of a comprehensive two-hybrid screen, tandem-affinity purification followed by mass spectrometry, and Northern analyses that Prp43p is associated with 90S, pre-60S, and pre-40S ribosomal particles- Prp43p seems preferentially associated with Pfa1p, a novel specific component of pre-40S ribosomal particles- In addition, Prp43p interacts with components of the RNA polymerase I -Pol I- transcription machinery and with mature 18S and 25S rRNAs- Hence, Prp43p might be delivered to nascent 90S ribosomal particles during pre-rRNA transcription and remain associated with preribosomal particles until their final maturation steps in the cytoplasm- Our data also suggest that the ATPase activity of Prp43p is required for early steps of pre-rRNA processing and normal accumulation of mature rRNAs- [PUBMED: 16227579] Copyright © 2009, Tyers Lab, The Samuel Lunenfeld Research Institute, Mount Sinai Hospital, All Rights Reserved. terms and conditions - privacy policy - Osprey Network Visualization System BioGRID: A General Repository for Interaction Datasets. Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers. Nucleic Acids Res. Jan 1;34:D535-9.