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          Institute: MPI für molekulare Zellbiologie und Genetik     Collection: Publikationen mpi-cbg 2003     Display Documents



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ID: 15658.0, MPI für molekulare Zellbiologie und Genetik / Publikationen mpi-cbg 2003
Targeting of U4/U6 small nuclear RNP assembly factor SART3/p110 to Cajal bodies
Authors:Stanek, D.; Rader, S. D.; Klingauf, M.; Neugebauer, K. M.
Language:English
Date of Publication (YYYY-MM-DD):2003-02-17
Title of Journal:Journal of Cell Biology
Journal Abbrev.:J. Cell Biol.
Volume:160
Issue / Number:4
Start Page:505
End Page:516
Review Status:Peer-review
Audience:Not Specified
Abstract / Description:The spliceosomal small nuclear RNAs (snRNAs) are distributed throughout the nucleoplasm and concentrated in nuclear inclusions termed Cajal bodies (CBs). A role for CBs in the metabolism of snRNPs has been proposed but is not well understood. The SART3/p110 protein interacts transiently with the U6 and U4/U6 snRNPs and promotes the reassembly of U4/U6 snRNPs after splicing in vitro. Here we report that SART3/p110 is enriched in CBs but not in gems or residual CBs lacking coilin. The U6 snRNP Sm-like (LSm) proteins, also involved in U4/U6 snRNP assembly, were localized to CBs as well. The levels of SART3/p110 and LSm proteins in CBs, were reduced upon treatment with the transcription inhibitor a-amanitin, suggesting that CB localization reflects active processes dependent on transcription/splicing. The NH2-terminal HAT domain of SART3/p110 was necessary and sufficient for specific protein targeting to CBs. Overexpression of truncation mutants containing the HAT domain had dominant negative effects on U6 snRNP localization to CBs, indicating that endogenous SART3/p110 plays a role in targeting the U6 snRNP to CBs. We propose that U4 and U6 snRNPs accumulate in CBs for the purpose of assembly into U4/U6 snRNPs by SART3/p110.
Free Keywords:RNA splicing; coiled (Cajal) body; U4/U6 small nuclear ribonucleoprotein; small nuclear RNA; nuclear proteins
Comment of the Author/Creator:Date: 2003, FEB 17
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für molekulare Zellbiologie und Genetik
External Affiliations:Max Planck Inst Mol Cell Biol & Genet, Pfotenhauerstr 108, D-; 01307 Dresden, Germany; Max Planck Inst Mol Cell Biol & Genet, D-01307 Dresden, Germany; Univ Calif San Francisco, Dept Biochem & Biophys, San Francisco, CA 94143 USA
Identifiers:ISI:000181090200005 [ID No:1]
ISSN:0021-9525 [ID No:2]
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