ArticleNucleic acids research2015
Domain organization within the nuclear export factor Mex67:Mtr2 generates an extended mRNA binding surface.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 31 citations in OpenAlex.
- Unraveling gene expression: a beginner's guide from chromatin modifications to mRNA export inNucleus (Austin, Tex.) · 2025Review
- From transcription to export: mRNA's winding path to the cytoplasm.Trends in biochemical sciences · 2025Review
- Characterization of a nuclear transport factor 2-like domain-containing protein in Plasmodium berghei.Malaria journal · 2024Article
- Article
- The Great Escape: mRNA Export through the Nuclear Pore Complex.International journal of molecular sciences · 2021Review
- Evolution and diversification of the nuclear pore complex.Biochemical Society transactions · 2021Review
- RNA Binding Proteins and Gene Expression Regulation inFrontiers in cellular and infection microbiology · 2020Article
- Mechanisms of nuclear mRNA export: A structural perspective.Traffic (Copenhagen, Denmark) · 2019Review
- Article
- The Nuclear Export Receptors TbMex67 and TbMtr2 Are Required for Ribosome Biogenesis in Trypanosoma brucei.mSphere · 2019Article
- Comparative analysis of plant MKK gene family reveals novel expansion mechanism of the members and sheds new light on functional conservation.BMC genomics · 2018Article
- The Trypanosoma cruzi RNA-binding protein RBP42 is expressed in the cytoplasm throughout the life cycle of the parasite.Parasitology research · 2018Article
- Ribosome-stalk biogenesis is coupled with recruitment of nuclear-export factor to the nascent 60S subunit.Nature structural & molecular biology · 2016Article
- Targeted cross-linking-mass spectrometry determines vicinal interactomes within heterogeneous RNP complexes.Nucleic acids research · 2016Article
- Structural Characterization of the Chaetomium thermophilum TREX-2 Complex and its Interaction with the mRNA Nuclear Export Factor Mex67:Mtr2.Structure (London, England : 1993) · 2015Article
- Structural characterization of the principal mRNA-export factor Mex67-Mtr2 from Chaetomium thermophilum.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Nuclear export of messenger RNA.Genes · 2015Review
- The principal mRNA nuclear export factor NXF1:NXT1 forms a symmetric binding platform that facilitates export of retroviral CTE-RNA.Nucleic acids research · 2015Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The Mex67:Mtr2 complex is the principal yeast nuclear export factor for bulk mRNA and also contributes to ribosomal subunit export. Mex67 is a modular protein constructed from four domains (RRM, LRR, NTF2-like and UBA) that have been thought to be joined by flexible linkers like beads on a string, with the RRM and LRR domains binding RNAs and the NTF2-like and UBA domains binding FG-nucleoporins to facilitate movement through nuclear pores. Here, we show that the NTF2-like domain from Saccharomyces cerevisiae Mex67:Mtr2 also contributes to RNA binding. Moreover, the 3.3 Å resolution crystal structure of the Mex67(ΔUBA):Mtr2 complex, supplemented with small angle X-ray scattering data, indicated that the LRR domain has a defined spatial relationship to the Mex67(NTF2L):Mtr2 region. Conversely, the RRM domain and especially the UBA domain are more mobile. The conformation assumed by the LRR and NTF2-like domains results in clusters of positively-charged residues on each becoming arranged to form a continuous interface for binding RNA on the opposite side of the complex to the region that interacts with FG-nucleoporins to facilitate passage through nuclear pores.
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Registered trials
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.