ArticleRNA (New York, N.Y.)2000
Substrate recognition by a eukaryotic RNase III: the double-stranded RNA-binding domain of Rnt1p selectively binds RNA containing a 5'-AGNN-3' tetraloop.
Article in RNA (New York, N.Y.), 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 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
33 citing papers in PubMed, 66 citations in OpenAlex.
- Article
- Processing of Potato Spindle Tuber Viroid RNAs in Yeast, a Nonconventional Host.Journal of virology · 2017Article
- The siRNA suppressor RTL1 is redox-regulated through glutathionylation of a conserved cysteine in the double-stranded-RNA-binding domain.Nucleic acids research · 2017Article
- Structure of a eukaryotic RNase III postcleavage complex reveals a double-ruler mechanism for substrate selection.Molecular cell · 2014Article
- Post-transcriptional regulation of iron homeostasis in Saccharomyces cerevisiae.International journal of molecular sciences · 2013Review
- RNA recognition by double-stranded RNA binding domains: a matter of shape and sequence.Cellular and molecular life sciences : CMLS · 2013Review
- Intrinsic dynamics of an extended hydrophobic core in the S. cerevisiae RNase III dsRBD contributes to recognition of specific RNA binding sites.Journal of molecular biology · 2013Article
- 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
- Features of double-stranded RNA-binding domains of RNA helicase A are necessary for selective recognition and translation of complex mRNAs.The Journal of biological chemistry · 2011Article
- Analysis of PKR-RNA interactions by sedimentation velocity.Methods in enzymology · 2011Article
- Short RNA duplexes guide sequence-dependent cleavage by human Dicer.RNA (New York, N.Y.) · 2010Article
- Analysis of PKR activation using analytical ultracentrifugation.Macromolecular bioscience · 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
- A method to find tissue-specific novel sites of selective adenosine deamination.Nucleic acids research · 2005Article
- Biochemical and genomic analysis of substrate recognition by the double-stranded RNA binding domain of yeast RNase III.RNA (New York, N.Y.) · 2005Article
- Genome-wide prediction and analysis of yeast RNase III-dependent snoRNA processing signals.Molecular and cellular biology · 2005Article
- Global analysis of yeast RNA processing identifies new targets of RNase III and uncovers a link between tRNA 5' end processing and tRNA splicing.Nucleic acids research · 2005Article
- The double-stranded-RNA-binding motif: interference and much more.Nature reviews. Molecular cell biology · 2004Review
- A cotranscriptional model for 3'-end processing of the Saccharomyces cerevisiae pre-ribosomal RNA precursor.RNA (New York, N.Y.) · 2004Article
- Dissecting the requirement for subgenomic promoter sequences by RNA recombination of brome mosaic virus in vivo: evidence for functional separation of transcription and recombination.Journal of virology · 2004Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Rnt1p is an RNase III homolog from budding yeast, required for processing snRNAs, snoRNAs, and rRNA. Numerous Rnt1p RNA substrates share potential to form a duplex structure with a terminal four-base loop with the sequence AGNN. Using a synthetic RNA modeled after the 25S rRNA 3' ETS cleavage site we find that the AGNN loop is an important determinant of substrate selectivity. When this loop sequence is altered, the rate of Rnt1p cleavage is reduced. The reduction in cleavage rate can be attributed to reduced binding of the mutant substrate as measured by a gel-shift assay. Deletion of the nonconserved N-terminal domain of Rnt1p does not affect cleavage site choice or the ability of the enzyme to distinguish substrates that contain the AGNN loop, indicating that this region is not required for selective cleavage. Strikingly, a recombinant fragment of Rnt1p containing little more than the dsRBD is able to discriminate between wild-type and mutant loop sequences in a binding assay. We propose that a major determinant of AGNN loop recognition by Rnt1p is present in its dsRBD.
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Registered trials
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.