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Structure of the nuclear exosome component Rrp6p reveals an interplay between the active site and the HRDC domain.
Midtgaard, Søren F; Assenholt, Jannie; Jonstrup, Anette Thyssen; Van, Lan B; Jensen, Torben Heick; Brodersen, Ditlev E.
Affiliation
  • Midtgaard SF; Centre for Structural Biology, Department of Molecular Biology, University of Aarhus, Gustav Wieds Vej 10c, DK-8000 Aarhus C, Denmark.
Proc Natl Acad Sci U S A ; 103(32): 11898-903, 2006 Aug 08.
Article in En | MEDLINE | ID: mdl-16882719
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.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Saccharomyces cerevisiae / Saccharomyces cerevisiae Proteins / Exoribonucleases Type of study: Prognostic_studies Language: En Journal: Proc Natl Acad Sci U S A Year: 2006 Document type: Article Affiliation country: Denmark

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Saccharomyces cerevisiae / Saccharomyces cerevisiae Proteins / Exoribonucleases Type of study: Prognostic_studies Language: En Journal: Proc Natl Acad Sci U S A Year: 2006 Document type: Article Affiliation country: Denmark