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

Michal Razew, Zbigniew Warkocki, Michal Taube, Adam Kolondra, Mariusz Czarnocki-Cieciura, Elzbieta Nowak, Karolina Labedzka-Dmoch, Aleksandra Kawinska, Jakub Piatkowski, Pawel Golik, Maciej Kozak, Andrzej Dziembowski and Marcin Nowotny ()
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Michal Razew: International Institute of Molecular and Cell Biology
Zbigniew Warkocki: 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: University of Warsaw
Aleksandra Kawinska: University of Warsaw
Jakub Piatkowski: University of Warsaw
Pawel Golik: Polish Academy of Sciences
Maciej Kozak: Adam Mickiewicz University
Andrzej Dziembowski: Polish Academy of Sciences
Marcin Nowotny: International Institute of Molecular and Cell Biology

Nature Communications, 2018, vol. 9, issue 1, 1-12

Abstract: 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.

Date: 2018
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DOI: 10.1038/s41467-017-02570-5

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