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Structural analysis of mtEXO mitochondrial RNA degradosome reveals tight coupling of nuclease and helicase components

DOI: 10.1038/s41467-017-02570-5 DOI Help

Authors: Michal Razew (International Institute of Molecular and Cell Biology) , Zbigniew Warkocki (Institute of Biochemistry and Biophysics, Polish Academy of Sciences) , Michal Taube (Adam Mickiewicz University) , Adam Kolondra (University of Warsaw) , Mariusz Czarnocki-Cieciura (International Institute of Molecular and Cell Biology) , Elzbieta Nowak (International Institute of Molecular and Cell Biology) , Karolina Labedzka-Dmoch (International Institute of Molecular and Cell Biology) , Aleksandra Kawinska (University of Warsaw) , Jakub Piatkowski (University of Warsaw) , Pawel Golik (University of Warsaw) , Maciej Kozak (Adam Mickiewicz University) , Andrzej Dziembowski (Polish Academy of Sciences) , Marcin Nowotny (International Institute of Molecular and Cell Biology)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 9

State: Published (Approved)
Published: January 2018

Open Access Open Access

Abstract: Nuclease and helicase activities play pivotal roles in various aspects of RNA processing and degradation. These two activities are often present in multi-subunit complexes from nucleic acid metabolism. In the mitochondrial exoribonuclease complex (mtEXO) both enzymatic activities are tightly coupled making it an excellent minimal system to study helicase–exoribonuclease coordination. mtEXO is composed of Dss1 3′-to-5′ exoribonuclease and Suv3 helicase. It is the master regulator of mitochondrial gene expression in yeast. Here, we present the structure of mtEXO and a description of its mechanism of action. The crystal structure of Dss1 reveals domains that are responsible for interactions with Suv3. Importantly, these interactions are compatible with the conformational changes of Suv3 domains during the helicase cycle. We demonstrate that mtEXO is an intimate complex which forms an RNA-binding channel spanning its entire structure, with Suv3 helicase feeding the 3′ end of the RNA toward the active site of Dss1.

Journal Keywords: Enzyme mechanisms; Multienzyme complexes; RNA decay; SAXS; X-ray crystallography

Diamond Keywords: Enzymes

Subject Areas: Biology and Bio-materials, Chemistry

Instruments: I04-Macromolecular Crystallography

Added On: 16/01/2018 16:09


Discipline Tags:

Biochemistry Genetics Chemistry Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)