Structure of the nuclear exosome component Rrp6p reveals an interplay between the active site and the HRDC domain

Søren Fuglsang Midtgaard, Jannie Assenholt, Anette Thyssen Jonstrup, Lan Bich Van, Torben Heick Jensen, Ditlev Egeskov Brodersen

    Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

    Abstract

    The multisubunit eukaryotic exosome is an essential RNA processing and degradation machine. In its nuclear form, the exosome associates with the auxiliary factor Rrp6p, which participates in both RNA processing and degradation reactions. The crystal structure of Saccharomyces cerevisiae Rrp6p displays a conserved RNase D core with a flanking HRDC (helicase and RNase D C-terminal) domain in an unusual conformation shown to be important for the processing function of the enzyme. Complexes with AMP and UMP, the products of the RNA degradation process, reveal how the protein specifically recognizes ribonucleotides and their bases. Finally, in vivo mutational studies show the importance of the domain contacts for the processing function of Rrp6p and highlight fundamental differences between the protein and its prokaryotic RNase D counterparts.
    Original languageEnglish
    JournalProceedings of the National Academy of Sciences
    Volume103
    Issue32
    Pages (from-to)11898-11903
    ISSN0027-8424
    Publication statusPublished - 2006

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