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    The cellular EJC interactome reveals higher-order mRNP structure and an EJC-SR protein nexus

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    Authors
    Singh, Guramrit
    Kucukural, Alper
    Cenik, Can
    Leszyk, John D.
    Shaffer, Scott A.
    Weng, Zhiping
    Moore, Melissa J.
    UMass Chan Affiliations
    Program in Bioinformatics and Integrative Biology
    Department of Biochemistry and Molecular Pharmacology
    Document Type
    Journal Article
    Publication Date
    2012-11-09
    Keywords
    *Exons
    Humans
    Multiprotein Complexes
    Proteome
    RNA Precursors
    *RNA Processing, Post-Transcriptional
    RNA Splicing
    Ribonucleoproteins
    Biochemistry, Biophysics, and Structural Biology
    Bioinformatics
    Computational Biology
    Genetics and Genomics
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    Link to Full Text
    http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3522173/
    Abstract
    In addition to sculpting eukaryotic transcripts by removing introns, pre-mRNA splicing greatly impacts protein composition of the emerging mRNP. The exon junction complex (EJC), deposited upstream of exon-exon junctions after splicing, is a major constituent of spliced mRNPs. Here, we report comprehensive analysis of the endogenous human EJC protein and RNA interactomes. We confirm that the major "canonical" EJC occupancy site in vivo lies 24 nucleotides upstream of exon junctions and that the majority of exon junctions carry an EJC. Unexpectedly, we find that endogenous EJCs multimerize with one another and with numerous SR proteins to form megadalton sized complexes in which SR proteins are super-stoichiometric to EJC core factors. This tight physical association may explain known functional parallels between EJCs and SR proteins. Further, their protection of long mRNA stretches from nuclease digestion suggests that endogenous EJCs and SR proteins cooperate to promote mRNA packaging and compaction.
    Source
    Cell. 2012 Nov 9;151(4):750-64. doi: 10.1016/j.cell.2012.10.007. Link to article on publisher's site
    DOI
    10.1016/j.cell.2012.10.007
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/25928
    PubMed ID
    23084401
    Related Resources
    Link to Article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1016/j.cell.2012.10.007
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