TREX exposes the RNA binding domain of Nxf1 to enable mRNA export

TREX exposes the RNA binding domain of Nxf1 to enable mRNA export

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 und...

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Main Authors: Viphakone, Nicolas, Hautbergue, Guillaume M., Walsh, Matthew, Chang, Chung-Te, Holland, Arthur, Folco, Eric G., Reed, Robin, Wilson, Stuart A.
Format: Online
Language:English
Published: 2012
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3654228/
id pubmed-3654228
recordtype oai_dc
spelling pubmed-36542282013-05-15 TREX exposes the RNA binding domain of Nxf1 to enable mRNA export Viphakone, Nicolas Hautbergue, Guillaume M. Walsh, Matthew Chang, Chung-Te Holland, Arthur Folco, Eric G. Reed, Robin Wilson, Stuart A. Article 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 drastically 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. 2012 /pmc/articles/PMC3654228/ /pubmed/22893130 http://dx.doi.org/10.1038/ncomms2005 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Viphakone, Nicolas
Hautbergue, Guillaume M.
Walsh, Matthew
Chang, Chung-Te
Holland, Arthur
Folco, Eric G.
Reed, Robin
Wilson, Stuart A.
spellingShingle Viphakone, Nicolas
Hautbergue, Guillaume M.
Walsh, Matthew
Chang, Chung-Te
Holland, Arthur
Folco, Eric G.
Reed, Robin
Wilson, Stuart A.
TREX exposes the RNA binding domain of Nxf1 to enable mRNA export
author_facet Viphakone, Nicolas
Hautbergue, Guillaume M.
Walsh, Matthew
Chang, Chung-Te
Holland, Arthur
Folco, Eric G.
Reed, Robin
Wilson, Stuart A.
author_sort Viphakone, Nicolas
title TREX exposes the RNA binding domain of Nxf1 to enable mRNA export
title_short TREX exposes the RNA binding domain of Nxf1 to enable mRNA export
title_full TREX exposes the RNA binding domain of Nxf1 to enable mRNA export
title_fullStr TREX exposes the RNA binding domain of Nxf1 to enable mRNA export
title_full_unstemmed TREX exposes the RNA binding domain of Nxf1 to enable mRNA export
title_sort trex exposes the rna binding domain of nxf1 to enable mrna export
description 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 drastically 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.
publishDate 2012
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3654228/
_version_ 1611977787225145344

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