ArticleMolecular biology of the cell2007
Coordination of Hpr1 and ubiquitin binding by the UBA domain of the mRNA export factor Mex67.
Article in Molecular biology of the cell, 2007. 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, 26 citations in OpenAlex.
- Structure of the human core transcription-export complex reveals a hub for multivalent interactions.eLife · 2020Article
- Mip6 binds directly to the Mex67 UBA domain to maintain low levels of Msn2/4 stress-dependent mRNAs.EMBO reports · 2019Article
- The Transcription Factor THO Promotes Transcription Initiation and Elongation by RNA Polymerase I.The Journal of biological chemistry · 2016Article
- 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
- To the pore and through the pore: a story of mRNA export kinetics.Biochimica et biophysica acta · 2012Review
- Architecture and nucleic acids recognition mechanism of the THO complex, an mRNP assembly factor.The EMBO journal · 2012Article
- H2B ubiquitylation controls the formation of export-competent mRNP.Molecular cell · 2012Article
- Structure and interaction of ubiquitin-associated domain of human Fas-associated factor 1.Protein science : a publication of the Protein Society · 2009Article
- 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.The Journal of biological chemistry · 2009Article
- A versatile interaction platform on the Mex67-Mtr2 receptor creates an overlap between mRNA and ribosome export.The EMBO journal · 2008Article
- The yeast THO complex forms a 5-subunit assembly that directly interacts with active chromatin.BioarchitectureArticle
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
The ubiquitin-associated (UBA) domain of the mRNA nuclear export receptor Mex67 helps in coordinating transcription elongation and nuclear export by interacting both with ubiquitin conjugates and specific targets, such as Hpr1, a component of the THO complex. Here, we analyzed substrate specificity and ubiquitin selectivity of the Mex67 UBA domain. UBA-Mex67 is formed by three helices arranged in a classical UBA fold plus a fourth helix, H4. Deletion or mutation of helix H4 strengthens the interaction between UBA-Mex67 and ubiquitin, but it decreases its affinity for Hpr1. Interaction with Hpr1 is required for Mex67 UBA domain to bind polyubiquitin, possibly by inducing an H4-dependent conformational change. In vivo, deletion of helix H4 reduces cotranscriptional recruitment of Mex67 on activated genes, and it also shows an mRNA export defect. Based on these results, we propose that H4 functions as a molecular switch that coordinates the interaction of Mex67 with ubiquitin bound to specific substrates, defines the selectivity of the Mex67 UBA domain for polyubiquitin, and prevents its binding to nonspecific substrates.
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