ArticleThe Journal of biological chemistry2010
In vitro activities of the multifunctional RNA silencing polymerase QDE-1 of Neurospora crassa.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Fungal small RNA: unveiling the breakthroughs and promising applications.Frontiers in fungal biology · 2025Review
- RDR1-mediated broad antitumor response: a novel strategy manipulating miRNAs as a powerful weapon.Life medicine · 2022Article
- Structural insights into the dual activities of the two-barrel RNA polymerase QDE-1.Nucleic acids research · 2022Article
- Article
- Article
- Functional Evolution in Orthologous Cell-encoded RNA-dependent RNA Polymerases.The Journal of biological chemistry · 2016Article
- Whole-genome RNAi screen highlights components of the endoplasmic reticulum/Golgi as a source of resistance to immunotoxin-mediated cytotoxicity.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- siRNA-directed DNA Methylation in Plants.Current genomics · 2015Article
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Authors and funding
5 authors.
Funding
Abstract
QDE-1 is an RNA- and DNA-dependent RNA polymerase that has functions in the RNA silencing and DNA repair pathways of the filamentous fungus Neurospora crassa. The crystal structure of the dimeric enzyme has been solved, and the fold of its catalytic core is related closely to that of eukaryotic DNA-dependent RNA polymerases. However, the specific activities of this multifunctional enzyme are still largely unknown. In this study, we characterized the in vitro activities of the N-terminally truncated QDE-1ΔN utilizing structure-based mutagenesis. Our results indicate that QDE-1 displays five distinct catalytic activities, which can be dissected by mutating critical amino acids or by altering reaction conditions. Our data also suggest that the RNA- and DNA-dependent activities have different modes for the initiation of RNA synthesis, which may reflect the mechanism that enables the polymerase to discriminate between template nucleic acids. Moreover, we show that QDE-1 is a highly potent terminal nucleotidyltransferase. Our results suggest that QDE-1 is able to regulate its activity mode depending on the template nucleic acid. This work extends our understanding of the biochemical properties of the QDE-1 enzyme and related RNA polymerases.
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