ArticleThe Journal of biological chemistry2009
Structural requirements for the ubiquitin-associated domain of the mRNA export factor Mex67 to bind its specific targets, the transcription elongation THO complex component Hpr1 and nucleoporin FXFG repeats.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 29 citations in OpenAlex.
- Division of labor in trypanosome RNA processing and export through expanded Mex67 paralogs.Nucleic acids research · 2026Article
- Mip6 binds directly to the Mex67 UBA domain to maintain low levels of Msn2/4 stress-dependent mRNAs.EMBO reports · 2019Article
- ORC interacts with THSC/TREX-2 and its subunits promote Nxf1 association with mRNP and mRNA export in Drosophila.Nucleic acids research · 2016Article
- An E2 accessory domain increases affinity for the anaphase-promoting complex and ensures E2 competition.The Journal of biological chemistry · 2015Article
- Structural characterization of the principal mRNA-export factor Mex67-Mtr2 from Chaetomium thermophilum.Acta crystallographica. Section F, Structural biology communications · 2015Article
- An agent-based model for mRNA export through the nuclear pore complex.Molecular biology of the cell · 2014Article
- The multifunctional nuclear pore complex: a platform for controlling gene expression.Current opinion in cell biology · 2014Review
- Regulation of gene expression by the ubiquitin-proteasome system.Seminars in cell & developmental biology · 2012Review
- Architecture and nucleic acids recognition mechanism of the THO complex, an mRNP assembly factor.The EMBO journal · 2012Article
- A model of a MAPK•substrate complex in an active conformation: a computational and experimental approach.PloS one · 2011Article
- The THO complex as a key mRNP biogenesis factor in development and cell differentiation.Journal of biology · 2010Article
- The yeast THO complex forms a 5-subunit assembly that directly interacts with active chromatin.BioarchitectureArticle
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
The ubiquitin-associated (UBA) domain of the principal Saccharomyces cerevisiae mRNA nuclear export factor, Mex67, can bind both nuclear pore protein (nucleoporin) FG repeats and Hpr1, a component of the TREX.THO complex that functions to link transcription and export. Using fluorescence resonance energy transfer-based assays, we show here that Hpr1 and the FG repeats interact with overlapping binding sites on the Mex67 UBA domain. We present the solution structure of the Mex67 UBA domain (UBA-Mex67) complexed with a FXFG nucleoporin peptide and define residues engaged in the interaction and those involved in the FXFG-induced conformational change. We show by NMR titration that the binding of Hpr1 produces analogous changes in chemical shifts in similar regions of the UBA domain. Together the data presented here indicate that both Hpr1 and FXFG nucleoporins may bind in a similar way to the UBA-Mex67 domain. However, whereas binding of Hpr1 allows UBA-Mex67 to interact with tetra-ubiquitin, the complex between UBA-Mex67 and FXFG is unable to bind mono- or tetra-ubiquitin, suggesting that both substrate binding and also the nature of the substrate may influence the affinity of the UBA-Mex67 domain for ubiquitin.
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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.