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Showing 1–5 of 5 results
Advanced filters: Author: Claire Basquin Clear advanced filters

  • The ASAP complex is emerging as an assembly of proteins at the interface between transcription, pre-mRNA splicing and mRNA quality control. Structural analysis of the ASAP core complex reveals macromolecular interactions between the subunits and their assembly into ASAP. In addition, ASAP subunits SAP18 and RNPS1 are shown to bind Pinin, forming a novel complex called PSAP.

    • Andrea Giovanni Murachelli
    • Judith Ebert
    • Elena Conti
    Research
    Nature Structural & Molecular Biology
    Volume: 19, P: 378-386

  • The DEAD-box protein DBP5 is involved in yeast mRNA export, though the mechanism by which it helps to remodel and release transcripts on the cytoplasmic face of the nuclear pore complex has been unclear. The structures of DBP5 in complex with the mRNA and AMPPNP, as well as with the nucleoporin NUP214, indicate that the transcript and nucleoporin compete for the same binding site, suggesting a model for the sequence of events occurring at the last step of export.

    • Holger von Moeller
    • Claire Basquin
    • Elena Conti
    Research
    Nature Structural & Molecular Biology
    Volume: 16, P: 247-254

  • Solving the crystal structure of an exosome complex from yeast, bound to different RNA substrates, offers insights into how the exosome can be utilized for precise processing of some 3′ ends, such as that of the 5.8S rRNA, while other RNAs are degraded to completion.

    • Debora Lika Makino
    • Benjamin Schuch
    • Elena Conti
    Research
    Nature
    Volume: 524, P: 54-58

  • The crystal structure of the putative exonuclease Exuperantia, required for Drosophila anterior patterning, reveals an EXO-SAM-like domain architecture that is catalytically inactive but mediates dimerization and RNA binding, which are essential for bicoid localization.

    • Daniela Lazzaretti
    • Katharina Veith
    • Fulvia Bono
    Research
    Nature Structural & Molecular Biology
    Volume: 23, P: 705-713