TREX exposes the RNA-binding domain of Nxf1 to enable mRNA export
Open Access
- 1 January 2012
- journal article
- research article
- Published by Springer Science and Business Media LLC in Nature Communications
- Vol. 3 (1), 1-14
- https://doi.org/10.1038/ncomms2005
Abstract
The metazoan TREX complex is recruited to mRNA during nuclear RNA processing and functions in exporting mRNA to the cytoplasm. Nxf1 is an mRNA export receptor, which binds processed mRNA and transports it through the nuclear pore complex. At present, the relationship between TREX and Nxf1 is not understood. Here we show that Nxf1 uses an intramolecular interaction to inhibit its own RNA-binding activity. When the TREX subunits Aly and Thoc5 make contact with Nxf1, Nxf1 is driven into an open conformation, exposing its RNA-binding domain, allowing RNA binding. Moreover, the combined knockdown of Aly and Thoc5 markedly reduces the amount of Nxf1 bound to mRNA in vivo and also causes a severe mRNA export block. Together, our data indicate that TREX provides a license for mRNA export by driving Nxf1 into a conformation capable of binding mRNA.This publication has 42 references indexed in Scilit:
- Ubiquitin-associated domain of Mex67 synchronizes recruitment of the mRNA export machinery with transcriptionProceedings of the National Academy of Sciences of the United States of America, 2006
- Molecular basis of RNA recognition and TAP binding by the SR proteins SRp20 and 9G8The EMBO Journal, 2006
- The solution structure of REF2-I reveals interdomain interactions and regions involved in binding mRNA export factors and RNARNA, 2006
- An intron with a constitutive transport element is retained in a Tap messenger RNANature, 2006
- Recruitment of the human TREX complex to mRNA during splicingGenes & Development, 2005
- Yra1p, a conserved nuclear RNA-binding protein, interacts directly with Mex67p and is required for mRNA exportThe EMBO Journal, 2000
- The Mex67p-mediated nuclear mRNA export pathway is conserved from yeast to humanThe EMBO Journal, 1999
- TAP binds to the constitutive transport element (CTE) through a novel RNA-binding motif that is sufficient to promote CTE-dependent RNA export from the nucleusThe EMBO Journal, 1999
- TAP, the Human Homolog of Mex67p, Mediates CTE-Dependent RNA Export from the NucleusMolecular Cell, 1998
- Mex67p, a novel factor for nuclear mRNA export, binds to both poly(A)+ RNA and nuclear poresThe EMBO Journal, 1997