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

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. Copyright © 2014 Elsevier Inc. All rights reserved.

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Emil Dedic, Paulina Seweryn, Anette Thyssen Jonstrup, Rasmus Koch Flygaard, Natalya U Fedosova, Søren Vrønning Hoffmann, Thomas Boesen, Ditlev Egeskov Brodersen. Structural analysis of the yeast exosome Rrp6p-Rrp47p complex by small-angle X-ray scattering. Biochemical and biophysical research communications. 2014 Jul 18;450(1):634-40

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PMID: 24937447

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