ArticleThe Journal of biological chemistry2013
Yeast Nab3 protein contains a self-assembly domain found in human heterogeneous nuclear ribonucleoprotein-C (hnRNP-C) that is necessary for transcription termination.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
- The Nrd1-Nab3-Sen1 transcription termination complex from a structural perspective.Biochemical Society transactions · 2023Review
- Insights into the Mechanism of Pre-mRNA Splicing of Tiny Introns from the Genome of a Giant CiliateInternational journal of molecular sciences · 2022Article
- Variable penetrance of Nab3 granule accumulation quantified by a new tool for high-throughput single-cell granule analysis.Current genetics · 2022Article
- Possible Role for Allelic Variation in YeastFrontiers in microbiology · 2021Article
- RNA Polymerase II CTD phosphatase Rtr1 fine-tunes transcription termination.PLoS genetics · 2020Article
- Nab3's localization to a nuclear granule in response to nutrient deprivation is determined by its essential prion-like domain.PloS one · 2018Article
- The structure of transcription termination factor Nrd1 reveals an original mode for GUAA recognition.Nucleic acids research · 2017Article
- The hnRNP-like Nab3 termination factor can employ heterologous prion-like domains in place of its own essential low complexity domain.PloS one · 2017Article
- Article
- Termination of Transcription of Short Noncoding RNAs by RNA Polymerase II.Annual review of biochemistry · 2015Review
- The exosome component Rrp6 is required for RNA polymerase II termination at specific targets of the Nrd1-Nab3 pathway.PLoS genetics · 2015Article
- Article
- A network of interdependent molecular interactions describes a higher order Nrd1-Nab3 complex involved in yeast transcription termination.The Journal of biological chemistry · 2013Article
- Aggregation of polyQ-extended proteins is promoted by interaction with their natural coiled-coil partners.BioEssays : news and reviews in molecular, cellular and developmental biology · 2013Article
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3 authors at 1 institution in 1 country.
Funding
Abstract
Nab3 is an RNA-binding protein whose function is important for terminating transcription by RNA polymerase II. It co-assembles with Nrd1, and the resulting heterodimer of these heterogeneous nuclear ribonucleoprotein-C (hnRNP)-like proteins interacts with the nascent transcript and RNA polymerase II. Previous genetic analysis showed that a short carboxyl-terminal region of Nab3 is functionally important for termination and is located far from the Nab3 RNA recognition domain in the primary sequence. The domain is structurally homologous to hnRNP-C from higher organisms. Here we provide biochemical evidence that this short region is sufficient to enable self-assembly of Nab3 into a tetrameric form in a manner similar to the cognate region of human hnRNP-C. Within this region, there is a stretch of low complexity protein sequence (16 glutamines) adjacent to a putative α-helix that potentiates the ability of the conserved region to self-assemble. The glutamine stretch and the final 18 amino acids of Nab3 are both important for termination in living yeast cells. The findings herein describe an additional avenue by which these hnRNP-like proteins can polymerize on target transcripts. This process is independent of, but acts in concert with, the interactions of the proteins with RNA and RNA polymerase and extends the relationship of Nab3 as a functional orthologue of a higher eukaryotic hnRNP.
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