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Updated: Apr 28, 2026
Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
Published on: January 10, 2018
Structural analysis of the yeast exosome Rrp6p-Rrp47p complex by small-angle X-ray scattering
Emil Dedic1, Paulina Seweryn1, Anette Thyssen Jonstrup1
1Centre for mRNP Biogenesis and Metabolism, Gustav Wieds Vej 10c, Aarhus University, DK-8000 Aarhus C, Denmark; Department of Molecular Biology and Genetics, Gustav Wieds Vej 10c, Aarhus University, DK-8000 Aarhus C, Denmark.
Abstract:
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.
