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Assays of the Helicase, ATPase, and Exoribonuclease Activities of the Yeast Mitochondrial Degradosome

Authors: Michal Malecki; Pawel Golik; Piotr P. Stepien;

Assays of the Helicase, ATPase, and Exoribonuclease Activities of the Yeast Mitochondrial Degradosome

Abstract

The mitochondrial degradosome (mtEXO) is the main enzymatic complex in RNA degradation, processing, and surveillance in Saccharomyces cerevisiae mitochondria. It consists of two nuclear-encoded subunits: the ATP-dependent RNA helicase Suv3p and the 3' to 5' exoribonuclease Dss1p. The two subunits depend on each other for their activity; the complex can therefore be considered as a model system for the cooperation of RNA helicases and exoribonucleases in RNA degradation. All the three activities of the complex (helicase, ATPase, and exoribonuclease) can be studied in vitro using recombinant proteins and protocols presented in this chapter.

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Keywords

Adenosine Triphosphatases, Polyribonucleotide Nucleotidyltransferase, Saccharomyces cerevisiae Proteins, Saccharomyces cerevisiae, Recombinant Proteins, Mitochondria, Protein Subunits, Multienzyme Complexes, Endoribonucleases, Exoribonucleases, Biological Assay, RNA Helicases

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citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
6
Average
Average
Average
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