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Chtop is a component of the dynamic TREX mRNA export complex
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Chtop is a component of the dynamic TREX mRNA export complex
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Journal Article
Chtop is a component of the dynamic TREX mRNA export complex
2013
Overview
The TREX complex couples nuclear pre‐mRNA processing with mRNA export and contains multiple protein components, including Uap56, Alyref, Cip29 and the multi‐subunit THO complex. Here, we have identified Chtop as a novel TREX component. We show that both Chtop and Alyref activate the ATPase and RNA helicase activities of Uap56 and that Uap56 functions to recruit both Alyref and Chtop onto mRNA. As observed with the THO complex subunit Thoc5, Chtop binds to the NTF2‐like domain of Nxf1, and this interaction requires arginine methylation of Chtop. Using RNAi, we show that co‐knockdown of Alyref and Chtop results in a potent mRNA export block. Chtop binds to Uap56 in a mutually exclusive manner with Alyref, and Chtop binds to Nxf1 in a mutually exclusive manner with Thoc5. However, Chtop, Thoc5 and Nxf1 exist in a single complex
in vivo
. Together, our data indicate that TREX and Nxf1 undergo dynamic remodelling, driven by the ATPase cycle of Uap56 and post‐translational modifications of Chtop.
The TREX complex coordinates nuclear mRNA processing and export. Chtop is a novel TREX component that stimulates the helicase activity of Uap56 and mediates Nxf1 binding to dynamically remodel mRNP export complexes.
Publisher
John Wiley & Sons, Ltd,Nature Publishing Group UK,Springer Nature B.V,Nature Publishing Group
Subject
/ C1ORF77
/ DEAD-box RNA Helicases - metabolism
/ EMBO36
/ Enzymes
/ Exodeoxyribonucleases - metabolism
/ Genetic Complementation Test
/ Humans
/ In Situ Hybridization, Fluorescence
/ Multiprotein Complexes - genetics
/ Multiprotein Complexes - metabolism
/ Nuclear Proteins - metabolism
/ Phosphoproteins - metabolism
/ Proteins
/ REF
/ RNA
/ RNA Processing, Post-Transcriptional - physiology
/ RNA-Binding Proteins - metabolism
/ TAP
