ArticleActa crystallographica. Section F, Structural biology communications2015
Structural characterization of the principal mRNA-export factor Mex67-Mtr2 from Chaetomium thermophilum.
Article in Acta crystallographica. Section F, Structural biology communications, 2015. 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, 29 citations in OpenAlex.
- Evolutionary, structural and functional insights in nuclear organisation and nucleocytoplasmic transport in trypanosomes.FEBS letters · 2023Review
- Identification and characterization of sugar-regulated promoters in Chaetomium thermophilum.BMC biotechnology · 2023Article
- Article
- Evolution and diversification of the nuclear pore complex.Biochemical Society transactions · 2021Review
- The nascent RNA binding complex SFiNX licenses piRNA-guided heterochromatin formation.Nature structural & molecular biology · 2019Article
- Interaction network of the ribosome assembly machinery from a eukaryotic thermophile.Protein science : a publication of the Protein Society · 2017Article
- Developing genetic tools to exploit Chaetomium thermophilum for biochemical analyses of eukaryotic macromolecular assemblies.Scientific reports · 2016Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Members of the Mex67-Mtr2/NXF-NXT1 family are the principal mediators of the nuclear export of mRNA. Mex67/NXF1 has a modular structure based on four domains (RRM, LRR, NTF2-like and UBA) that are thought to be present across species, although the level of sequence conservation between organisms, especially in lower eukaryotes, is low. Here, the crystal structures of these domains from the thermophilic fungus Chaetomium thermophilum are presented together with small-angle X-ray scattering (SAXS) and in vitro RNA-binding data that indicate that, not withstanding the limited sequence conservation between different NXF family members, the molecules retain similar structural and RNA-binding properties. Moreover, the resolution of crystal structures obtained with the C. thermophilum domains was often higher than that obtained previously and, when combined with solution and biochemical studies, provided insight into the structural organization, self-association and RNA-binding properties of Mex67-Mtr2 that facilitate mRNA nuclear export.
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