Structural analysis of the yeast exosome Rrp6p-Rrp47p complex by small-angle x-ray scattering

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  • Emil Dedic, Centre for mRNP Biogenesis and Metabolism; Department of Molecular Biology and Genetics, Gustav Wieds Vej 10c, Ny Munkegade 120, Aarhus University, DK-8000 Aarhus C, Denmark., Danmark
  • Paulina Seweryn, Centre for mRNP Biogenesis and Metabolism; Department of Molecular Biology and Genetics, Gustav Wieds Vej 10c, Ny Munkegade 120, Aarhus University, DK-8000 Aarhus C, Denmark., Danmark
  • Anette Thyssen Jonstrup, Centre for mRNP Biogenesis and Metabolism; Department of Molecular Biology and Genetics, Gustav Wieds Vej 10c, Ny Munkegade 120, Aarhus University, DK-8000 Aarhus C, Denmark., Danmark
  • Rasmus Koch Flygaard, Centre for mRNP Biogenesis and Metabolism; Department of Molecular Biology and Genetics, Gustav Wieds Vej 10c, Ny Munkegade 120, Aarhus University, DK-8000 Aarhus C, Denmark., Danmark
  • Natalya U Fedosova
  • Søren Vrønning Hoffmann
  • Thomas Boesen
  • Ditlev E. Brodersen

The RNase D-type 3'-5' exonuclease Rrp6p from Saccharomyces cerevisiae is a nuclear-specific cofactor of the RNA exosome and associates in vivo with Rrp47p (Lrp1p). Here, we show using biochemistry and small-angle x-ray scattering (SAXS) that Rrp6p and Rrp47p associate into a stable, heterodimeric complex with an elongated shape consistent with binding of Rrp47p to the nuclease domain and opposite of the HRDC domain of Rrp6p. Rrp47p reduces the exonucleolytic activity of Rrp6p on both single-stranded and structured RNA substrates without significantly altering the affinity towards RNA or the ability of Rrp6p to degrade RNA secondary structure.

OriginalsprogEngelsk
TidsskriftBiochemical and Biophysical Research Communications
Vol/bind450
Nummer1
Sider (fra-til)634-640
Antal sider7
ISSN0006-291X
DOI
StatusUdgivet - 18 jul. 2014

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