ArticlePlant molecular biology2003
Arabidopsis transportin1 is the nuclear import receptor for the circadian clock-regulated RNA-binding protein AtGRP7.
Article in Plant molecular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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29 citing papers in PubMed, 68 citations in OpenAlex.
- The glycine-rich domain of GRP7 plays a crucial role in binding long RNAs and facilitating phase separation.Scientific reports · 2024Article
- Characterization of Almond Scion/Rootstock Communication in Cultivar and Rootstock Tissues through an RNA-Seq Approach.Plants (Basel, Switzerland) · 2023Article
- Identification of the Karyopherin Superfamily in Maize and Its Functional Cues in Plant Development.International journal of molecular sciences · 2022Review
- Variations in Circadian Clock Organization & Function: A Journey from Ancient to Recent.Planta · 2022Review
- OsGRP3 Enhances Drought Resistance by Altering Phenylpropanoid Biosynthesis Pathway in Rice (International journal of molecular sciences · 2022Article
- The emerging role of biomolecular condensates in plant immunity.The Plant cell · 2022Article
- Article
- Integrative Proteomic and Phosphoproteomic Analyses of Pattern- and Effector-Triggered Immunity in Tomato.Frontiers in plant science · 2021Article
- The Unusual Suspects in Cytokinesis: Fitting the Pieces Together.Frontiers in cell and developmental biology · 2020Review
- Beyond Transcription: Fine-Tuning of Circadian Timekeeping by Post-Transcriptional Regulation.Genes · 2018Review
- Nictaba Homologs fromFrontiers in plant science · 2017Article
- Comparative proteomic analysis of the shoot apical meristem in maize between a ZmCCT-associated near-isogenic line and its recurrent parent.Scientific reports · 2016Article
- Genome-wide identification and phylogenetic analysis of plant RNA binding proteins comprising both RNA recognition motifs and contiguous glycine residues.Molecular genetics and genomics : MGG · 2016Article
- Identification of potential cargo proteins of transportin protein AtTRN1 in Arabidopsis thaliana.Plant cell reports · 2016Article
- Overexpression ofFrontiers in plant science · 2016Article
- Age-related expression analysis of mouse liver nuclear protein binding to 3'-untranslated region of Period2 gene.The journal of physiological sciences : JPS · 2015Article
- Circadian rhythms and post-transcriptional regulation in higher plants.Frontiers in plant science · 2015Review
- Structural basis of nucleic acid binding by Nicotiana tabacum glycine-rich RNA-binding protein: implications for its RNA chaperone function.Nucleic acids research · 2014Article
- A glycine-rich RNA-binding protein affects gibberellin biosynthesis in Arabidopsis.Molecular biology reports · 2014Article
- Pseudomonas HopU1 modulates plant immune receptor levels by blocking the interaction of their mRNAs with GRP7.The EMBO journal · 2013Article
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4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We characterized the Arabidopsis orthologue of the human nuclear import receptor transportin1 (TRN1). Like the human receptor, Arabidopsis TRN1 recognizes nuclear import signals on proteins that are different from the classical basic nuclear localization signals. The M9 domain of human heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) is the prototype of such signals. We show that AtTRN1 binds to similar domains in hnRNP-like proteins from plants. AtTRN1 also interacts with human hnRNP A1 and with yeast Nab2p, two classical import cargo proteins of transportin in these organisms. Like all nuclear transport receptors of the importin-beta family, AtTRN1 binds to the regulatory GTPase Ran from Arabidopsis. We demonstrated that the amino terminus of AtTRN1 is necessary for this interaction. Recombinant AtTRN1 conferred nuclear import of fluorescently labelled BSA-M9 peptide conjugates in permeabilized HeLa cells, functionally replacing human TRN1 in these in vitro nuclear import assays. We identified three plant substrate proteins that interact with AtTRN1 and contain M9-like domains: a novel Arabidopsis hnRNP that shows high similarity to human hnRNP A1 and two small RNA-binding proteins from Arabidopsis, AtGRP7 and AtGRP8. Nuclear import activity of the M9-like domains of these plant proteins was demonstrated in vivo by their ability to confer partial nuclear re-localisation of a GFP fusion protein containing a nuclear export signal. In addition, fluorescently labelled AtGRP7 was specifically imported into nuclei of permeabilized HeLa cells by Arabidopsis AtTRN1 and human TRN1. These results suggest that the transportin-mediated nuclear import pathway is highly conserved between man, yeast and plants.
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