ArticleMolecular biology of the cell2004
Cell cycle-dependent nuclear localization of yeast RNase III is required for efficient cell division.
Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 38 citations in OpenAlex.
- Article
- Ribonucleases in Mendelian disease: Characterization and insight from model organisms.Genes & diseases · 2025Review
- Efficient termination of transcription by RNA polymerase I requires a conserved hairpin of the ribosomal RNA precursor.Science advances · 2025Article
- Stress-induced inhibition of mRNA export triggers RNase III-mediated decay of theRNA (New York, N.Y.) · 2021Article
- Review
- Promoter-dependent nuclear RNA degradation ensures cell cycle-specific gene expression.Communications biology · 2019Article
- Transcriptome wide annotation of eukaryotic RNase III reactivity and degradation signals.PLoS genetics · 2015Article
- Post-transcriptional regulation of iron homeostasis in Saccharomyces cerevisiae.International journal of molecular sciences · 2013Review
- RNA-dependent regulation of the cell wall stress response.Nucleic acids research · 2012Article
- Quality control of MATa1 splicing and exon skipping by nuclear RNA degradation.Nucleic acids research · 2012Article
- Reporter mRNAs cleaved by Rnt1p are exported and degraded in the cytoplasm.Nucleic acids research · 2011Article
- A synthetic library of RNA control modules for predictable tuning of gene expression in yeast.Molecular systems biology · 2011Article
- An Ascovirus-encoded RNase III autoregulates its expression and suppresses RNA interference-mediated gene silencing.Journal of virology · 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
- Short RNA guides cleavage by eukaryotic RNase III.PloS one · 2007Article
- Loc1p is required for efficient assembly and nuclear export of the 60S ribosomal subunit.Molecular genetics and genomics : MGG · 2006Article
- Exploring the functions of RNA interference pathway proteins: some functions are more RISCy than others?The Biochemical journal · 2005Review
- Genome-wide prediction and analysis of yeast RNase III-dependent snoRNA processing signals.Molecular and cellular biology · 2005Article
- A cotranscriptional model for 3'-end processing of the Saccharomyces cerevisiae pre-ribosomal RNA precursor.RNA (New York, N.Y.) · 2004Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Members of the double-stranded RNA-specific ribonuclease III (RNase III) family were shown to affect cell division and chromosome segregation, presumably through an RNA interference-dependent mechanism. Here, we show that in Saccharomyces cerevisiae, where the RNA interference machinery is not conserved, an orthologue of RNase III (Rnt1p) is required for progression of the cell cycle and nuclear division. The deletion of Rnt1p delayed cells in both G1 and G2/M phases of the cell cycle. Nuclear division and positioning at the bud neck were also impaired in Deltarnt1 cells. The cell cycle defects were restored by the expression of catalytically inactive Rnt1p, indicating that RNA cleavage is not essential for cell cycle progression. Rnt1p was found to exit from the nucleolus to the nucleoplasm in the G2/M phase, and perturbation of its localization pattern delayed the progression of cell division. A single mutation in the Rnt1p N-terminal domain prevented its accumulation in the nucleoplasm and slowed exit from mitosis without any detectable effects on RNA processing. Together, the data reveal a new role for a class II RNase III in the cell cycle and suggest that at least some members of the RNase III family possess catalysis-independent functions.
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