Small-angle x-ray scattering structures of the Rrp6p-Rrp47p complex

Structure of the Rrp6p-Rrp47p complex by SAXS

Structure of the Rrp6p-Rrp47p complex by SAXS

Today, our lab has published structural and functional studies of the yeast exosome Rrp6p-Rrp47p complex in Biochem. Biophys. Res. Commun. In this paper, we show how the two proteins, despite the fact that they both multimerise, form a stable 1:1 complex with Rrp47p situated on the “top” of the Rrp6p exonuclease domain. RNA degradation experiments with and without Rrp47p present further show that the co-factor has a very limited effect on the activity and specificity of the nuclease. Together, our data suggest a role for Rrp47p in higher-order organisation of the exosome complex, perhaps linked to interactions with other protein factors.

For more information, have a look at the paper in Biochem. Biophys. Res. Commun.

Dedic E., Seweryn P., Jonstrup A. T., Flygaard R. K., Fedosova N. U., Hoffmann S. V., Boesen T.,Brodersen D. E. (2014), “Structural analysis of the yeast exosome Rrp6p-Rrp47p complex by small-angle X-ray scattering”, Biochem Biophys Res Commun, 450(1):634-40.