ArticleThe EMBO journal2004
A new alpha-helical extension promotes RNA binding by the dsRBD of Rnt1p RNAse III.
Article in The EMBO journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Review
- Molecular basis for transfer RNA recognition by the double-stranded RNA-binding domain of human dihydrouridine synthase 2.Nucleic acids research · 2019Article
- The siRNA suppressor RTL1 is redox-regulated through glutathionylation of a conserved cysteine in the double-stranded-RNA-binding domain.Nucleic acids research · 2017Article
- A bimodular nuclear localization signal assembled via an extended double-stranded RNA-binding domain acts as an RNA-sensing signal for transportin 1.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Engineering RNA-binding proteins for biology.The FEBS journal · 2013Review
- 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
- Solution structure of the N-terminal dsRBD of Drosophila ADAR and interaction studies with RNA.Biochimie · 2012Article
- Modular protein-RNA interactions regulating mRNA metabolism: a role for NMR.European biophysics journal : EBJ · 2011Review
- An extended dsRBD with a novel zinc-binding motif mediates nuclear retention of fission yeast Dicer.The EMBO journal · 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
- Analysis of PKR-RNA interactions by sedimentation velocity.Methods in enzymology · 2011Article
- Dynamic origins of differential RNA binding function in two dsRBDs from the miRNA "microprocessor" complex.Biochemistry · 2010Article
- Novel protein-protein contacts facilitate mRNA 3'-processing signal recognition by Rna15 and Hrp1.Journal of molecular biology · 2010Article
- Article
- Characterization of a ribonuclease III-like protein required for cleavage of the pre-rRNA in the 3'ETS in Arabidopsis.Nucleic acids research · 2008Article
- Site-directed spin labeling studies on nucleic acid structure and dynamics.Progress in nucleic acid research and molecular biology · 2008Review
- Deletion of Rnt1p alters the proportion of open versus closed rRNA gene repeats in yeast.Molecular and cellular biology · 2008Article
Corrections and comments
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Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rnt1 endoribonuclease, the yeast homolog of RNAse III, plays an important role in the maturation of a diverse set of RNAs. The enzymatic activity requires a conserved catalytic domain, while RNA binding requires the double-stranded RNA-binding domain (dsRBD) at the C-terminus of the protein. While bacterial RNAse III enzymes cleave double-stranded RNA, Rnt1p specifically cleaves RNAs that possess short irregular stem-loops containing 12-14 base pairs interrupted by internal loops and bulges and capped by conserved AGNN tetraloops. Consistent with this substrate specificity, the isolated Rnt1p dsRBD and the 30-40 amino acids that follow bind to AGNN-containing stem-loops preferentially in vitro. In order to understand how Rnt1p recognizes its cognate processing sites, we have defined its minimal RNA-binding domain and determined its structure by solution NMR spectroscopy and X-ray crystallography. We observe a new carboxy-terminal helix following a canonical dsRBD structure. Removal of this helix reduces binding to Rnt1p substrates. The results suggest that this helix allows the Rnt1p dsRBD to bind to short RNA stem-loops by modulating the conformation of helix alpha1, a key RNA-recognition element of the dsRBD.
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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.