Structure of a cytoplasmic 11-subunit RNA exosome complex

 

Eva Kowalinski, Alexander Kögel, Judith Ebert, Peter Reichelt, Elisabeth Stegmann, Bianca Habermann, Elena Conti

Molecular Cell
2016 vol: 63 issue: 1 pp: 125-134 doi: 10.1016/j.molcel.2016.05.028

Abstract
The RNA exosome complex associates with nuclear and cytoplasmic cofactors to mediate the decay, surveillance, or processing of a wide variety of transcripts. In the cytoplasm, the conserved core of the exosome (Exo10) functions together with the conserved Ski complex. The interaction of S. cerevisiae Exo10 and Ski is not direct but requires a bridging cofactor, Ski7. Here, we report the 2.65 Å resolution structure of S. cerevisiae Exo10 bound to the interacting domain of Ski7. Extensive hydrophobic interactions rationalize the high affinity and stability of this complex, pointing to Ski7 as a constitutive component of the cytosolic exosome. Despite the absence of sequence homology, cytoplasmic Ski7 and nuclear Rrp6 bind Exo10 using similar surfaces and recognition motifs. Knowledge of the interacting residues in the yeast complexes allowed us to identify a splice variant of human HBS1-Like as a Ski7-like exosome-binding protein, revealing the evolutionary conservation of this cytoplasmic cofactor.

View Publication

Topics: Fusion proteins, High affinity, High impact journal, Peptides, Supplements, Monolith – MicroScale Thermophoresis, MST, Proteins, Publications

 

 

Previous Article
Twenty years on: the impact of fragments on drug discovery
Twenty years on: the impact of fragments on drug discovery

Next Article
Binding properties of YjeQ (RsgA), RbfA, RimM and Era to assembly intermediates of the 30S subunit
Binding properties of YjeQ (RsgA), RbfA, RimM and Era to assembly intermediates of the 30S subunit

×

Sign up to receive
the latest NanoTemper news, product updates, event announcements and more

First Name
Last Name
Company Name
State
Province
State
Region
State
Canton
Agree to Privacy Policy*
*I have fully read, understood and agree to the Privacy Policy. I accept the storing and processing of my personal data by NanoTemper as described in the Privacy Policy.

By completing this form, you provide us consent to contact you with educational content, news and information about our products, services and events. You may unsubscribe at any time.
Thank you!
Error - something went wrong!