The N-terminal domain that distinguishes yeast from bacterial RNase III contains a dimerization signal required for efficient double-stranded RNA cleavage.
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SRp30c is a repressor of 3' splice site utilization.Ribonuclease III mechanisms of double-stranded RNA cleavageSolution structure of conserved AGNN tetraloops: insights into Rnt1p RNA processingStructure of a Yeast RNase III dsRBD Complex with a Noncanonical RNA Substrate Provides New Insights into Binding Specificity of dsRBDsThe Inside-Out Mechanism of Dicers from Budding YeastsStructure of a Eukaryotic RNase III Postcleavage Complex Reveals a Double-Ruler Mechanism for Substrate SelectionDeletion of Rnt1p alters the proportion of open versus closed rRNA gene repeats in yeastMultiple protein/protein and protein/RNA interactions suggest roles for yeast DNA/RNA helicase Sen1p in transcription, transcription-coupled DNA repair and RNA processing.Cell cycle-dependent nuclear localization of yeast RNase III is required for efficient cell division.Interactions of Sen1, Nrd1, and Nab3 with multiple phosphorylated forms of the Rpb1 C-terminal domain in Saccharomyces cerevisiae.Characterization of a ribonuclease III-like protein required for cleavage of the pre-rRNA in the 3'ETS in ArabidopsisSen1p performs two genetically separable functions in transcription and processing of U5 small nuclear RNA in Saccharomyces cerevisiaeA synthetic library of RNA control modules for predictable tuning of gene expression in yeast.Synthetic RNA modules for fine-tuning gene expression levels in yeast by modulating RNase III activity.Substrate recognition by a eukaryotic RNase III: the double-stranded RNA-binding domain of Rnt1p selectively binds RNA containing a 5'-AGNN-3' tetraloop.A cotranscriptional model for 3'-end processing of the Saccharomyces cerevisiae pre-ribosomal RNA precursor.Biochemical and genomic analysis of substrate recognition by the double-stranded RNA binding domain of yeast RNase III.An ADAR that edits transcripts encoding ion channel subunits functions as a dimer.The catalytic efficiency of yeast ribonuclease III depends on substrate specific product release rateThe Functional Cycle of Rnt1p: Five Consecutive Steps of Double-Stranded RNA Processing by a Eukaryotic RNase III.Comparison of preribosomal RNA processing pathways in yeast, plant and human cells - focus on coordinated action of endo- and exoribonucleases.A physical interaction between Gar1p and Rnt1pi is required for the nuclear import of H/ACA small nucleolar RNA-associated proteins.Multimerization of Staufen1 in live cells.A new alpha-helical extension promotes RNA binding by the dsRBD of Rnt1p RNAse III.Genome-wide prediction and analysis of yeast RNase III-dependent snoRNA processing signals.The siRNA suppressor RTL1 is redox-regulated through glutathionylation of a conserved cysteine in the double-stranded-RNA-binding domain.Conserved Proteins of the RNA Interference System in the Arbuscular Mycorrhizal Fungus Rhizoglomus irregulare Provide New Insight into the Evolutionary History of Glomeromycota.Both N-terminal catalytic and C-terminal RNA binding domain contribute to substrate specificity and cleavage site selection of RNase III.An Arabidopsis RNase III-like protein, AtRTL2, cleaves double-stranded RNA in vitro.Evaluation of the RNA determinants for bacterial and yeast RNase III binding and cleavage.One functional subunit is sufficient for catalytic activity and substrate specificity of Escherichia coli endoribonuclease III artificial heterodimers.
P2860
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P2860
The N-terminal domain that distinguishes yeast from bacterial RNase III contains a dimerization signal required for efficient double-stranded RNA cleavage.
description
2000 nî lūn-bûn
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2000年の論文
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2000年論文
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2000年論文
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2000年論文
@zh-hk
2000年論文
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2000年論文
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name
The N-terminal domain that dis ...... double-stranded RNA cleavage.
@en
type
label
The N-terminal domain that dis ...... double-stranded RNA cleavage.
@en
prefLabel
The N-terminal domain that dis ...... double-stranded RNA cleavage.
@en
P2093
P2860
P1476
The N-terminal domain that dis ...... double-stranded RNA cleavage.
@en
P2093
Abou Elela S
Lamontagne B
Tremblay A
P2860
P304
P356
10.1128/MCB.20.4.1104-1115.2000
P407
P577
2000-02-01T00:00:00Z