ArticleMolecular and cellular biology2000
The N-terminal domain that distinguishes yeast from bacterial RNase III contains a dimerization signal required for efficient double-stranded RNA cleavage.
Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 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
31 citing papers in PubMed, 53 citations in OpenAlex.
- RNase III, Ribosome Biogenesis and Beyond.Microorganisms · 2021Review
- Structural and mechanistic insight into stem-loop RNA processing by yeast Pichia stipitis Dicer.Protein science : a publication of the Protein Society · 2021Article
- Dicer 1 ofVirusdisease · 2019Article
- Saccharomyces cerevisiae (Baker's Yeast) as an Interfering RNA Expression and Delivery System.Current drug targets · 2019Review
- Conserved Proteins of the RNA Interference System in the Arbuscular Mycorrhizal Fungus Rhizoglomus irregulare Provide New Insight into the Evolutionary History of Glomeromycota.Genome biology and evolution · 2018Article
- The siRNA suppressor RTL1 is redox-regulated through glutathionylation of a conserved cysteine in the double-stranded-RNA-binding domain.Nucleic acids research · 2017Article
- The Functional Cycle of Rnt1p: Five Consecutive Steps of Double-Stranded RNA Processing by a Eukaryotic RNase III.Structure (London, England : 1993) · 2017Article
- The catalytic efficiency of yeast ribonuclease III depends on substrate specific product release rate.Nucleic acids research · 2016Article
- Structure of a eukaryotic RNase III postcleavage complex reveals a double-ruler mechanism for substrate selection.Molecular cell · 2014Article
- Interactions of Sen1, Nrd1, and Nab3 with multiple phosphorylated forms of the Rpb1 C-terminal domain in Saccharomyces cerevisiae.Eukaryotic cell · 2012Article
- Synthetic RNA modules for fine-tuning gene expression levels in yeast by modulating RNase III activity.Nucleic acids research · 2011Article
- Article
- Structure of a yeast RNase III dsRBD complex with a noncanonical RNA substrate provides new insights into binding specificity of dsRBDs.Structure (London, England : 1993) · 2011Article
- An Arabidopsis RNase III-like protein, AtRTL2, cleaves double-stranded RNA in vitro.Journal of plant research · 2011Article
- A synthetic library of RNA control modules for predictable tuning of gene expression in yeast.Molecular systems biology · 2011Article
- Multimerization of Staufen1 in live cells.RNA (New York, N.Y.) · 2010Article
- Sen1p performs two genetically separable functions in transcription and processing of U5 small nuclear RNA in Saccharomyces cerevisiae.Genetics · 2010Article
- Characterization of a ribonuclease III-like protein required for cleavage of the pre-rRNA in the 3'ETS in Arabidopsis.Nucleic acids research · 2008Article
- Deletion of Rnt1p alters the proportion of open versus closed rRNA gene repeats in yeast.Molecular and cellular biology · 2008Article
- Biochemical and genomic analysis of substrate recognition by the double-stranded RNA binding domain of yeast RNase III.RNA (New York, N.Y.) · 2005Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Yeast Rnt1 is a member of the double-stranded RNA (dsRNA)-specific RNase III family identified by conserved dsRNA binding (dsRBD) and nuclease domains. Comparative sequence analyses have revealed an additional N-terminal domain unique to the eukaryotic homologues of RNase III. The deletion of this domain from Rnt1 slowed growth and led to mild accumulation of unprocessed 25S pre-rRNA. In vitro, deletion of the N-terminal domain reduced the rate of RNA cleavage under physiological salt concentration. Size exclusion chromatography and cross-linking assays indicated that the N-terminal domain and the dsRBD self-interact to stabilize the Rnt1 homodimer. In addition, an interaction between the N-terminal domain and the dsRBD was identified by a two-hybrid assay. The results suggest that the eukaryotic N-terminal domain of Rnt1 ensures efficient dsRNA cleavage by mediating the assembly of optimum Rnt1-RNA ribonucleoprotein complex.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.