ArticleNucleic acids research2017
The structure of transcription termination factor Nrd1 reveals an original mode for GUAA recognition.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 16 citations in OpenAlex.
- DeepPANB: integrating protein language model with PaiNN equivariant graph neural networks for prediction of protein-nucleic acid binding sites.Briefings in bioinformatics · 2026Article
- Overexpression of the RNA-binding protein NrdA affects global gene expression and secondary metabolism inmSphere · 2025Article
- The Nrd1-Nab3-Sen1 transcription termination complex from a structural perspective.Biochemical Society transactions · 2023Review
- Structural basis of Nrd1-Nab3 heterodimerization.Life science alliance · 2022Article
- A Genome-Wide Screen Reveals That Endocytic Genes Are Important for Pma1p Asymmetry during Cell Division inInternational journal of molecular sciences · 2022Article
- Genetic screen for suppression of transcriptional interference identifies a gain-of-function mutation in Pol2 termination factor Seb1.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Identification of Three Sequence Motifs in the Transcription Termination Factor Sen1 that Mediate Direct Interactions with Nrd1.Structure (London, England : 1993) · 2019Article
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Authors and funding
10 authors at 4 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Transcription termination of non-coding RNAs is regulated in yeast by a complex of three RNA binding proteins: Nrd1, Nab3 and Sen1. Nrd1 is central in this process by interacting with Rbp1 of RNA polymerase II, Trf4 of TRAMP and GUAA/G terminator sequences. We lack structural data for the last of these binding events. We determined the structures of Nrd1 RNA binding domain and its complexes with three GUAA-containing RNAs, characterized RNA binding energetics and tested rationally designed mutants in vivo. The Nrd1 structure shows an RRM domain fused with a second α/β domain that we name split domain (SD), because it is formed by two non-consecutive segments at each side of the RRM. The GUAA interacts with both domains and with a pocket of water molecules, trapped between the two stacking adenines and the SD. Comprehensive binding studies demonstrate for the first time that Nrd1 has a slight preference for GUAA over GUAG and genetic and functional studies suggest that Nrd1 RNA binding domain might play further roles in non-coding RNAs transcription termination.
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