ArticleBiochemical and biophysical research communications2009
Characterization of the Drosophila melanogaster Dis3 ribonuclease.
Article in Biochemical and biophysical research communications, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- Molecular determinants of metazoan tricRNA biogenesis.Nucleic acids research · 2019Article
- The mitochondrial RNA landscape of Saccharomyces cerevisiae.PloS one · 2013Article
- Dis3- and exosome subunit-responsive 3' mRNA instability elements.Biochemical and biophysical research communications · 2012Article
- Pronounced and extensive microtubule defects in a Saccharomyces cerevisiae DIS3 mutant.Yeast (Chichester, England) · 2011Article
- The exozyme model: a continuum of functionally distinct complexes.RNA (New York, N.Y.) · 2011Review
- Drosophila melanogaster Dis3 N-terminal domains are required for ribonuclease activities, nuclear localization and exosome interactions.Nucleic acids research · 2010Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The Dis3 ribonuclease is a member of the hydrolytic RNR protein family. Although much progress has been made in understanding the structure, function, and enzymatic activities of prokaryotic RNR family members RNase II and RNase R, there are no activity studies of the metazoan ortholog, Dis3. Here, we characterize the activity of the Drosophila melanogaster Dis3 (dDis3) protein. We find that dDis3 is active in the presence of various monovalent and divalent cations, and requires divalent cations for activity. dDis3 hydrolyzes compositionally distinct RNA substrates, yet releases different products depending upon the substrate. Additionally, dDis3 remains active when lacking N-terminal domains, suggesting that an independent active site resides in the C-terminus of the protein. Finally, a study of dDis3 interactions with dRrp6 and core exosome subunits in extracts revealed sensitivity to higher divalent cation concentrations and detergent, suggesting the presence of both ionic and hydrophobic interactions in dDis3-exosome complexes. Our study thus broadens our mechanistic understanding of the general ribonuclease activity of Dis3 and RNR family members.
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Registered trials
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