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Structural basis for binding the TREX2 complex to nuclear pores, GAL1 localisation and mRNA export
The conserved Sac3:Thp1:Sem1:Sus1:Cdc31 (TREX2) complex binds to nuclear pore complexes (NPCs) and, in addition to integrating mRNA nuclear export with preceding steps in the gene expression pathway, facilitates re-positioning of highly regulated actively transcribing genes (such as GAL1) to NPCs. A...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4041426/ https://www.ncbi.nlm.nih.gov/pubmed/24705649 http://dx.doi.org/10.1093/nar/gku252 |
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author | Jani, Divyang Valkov, Eugene Stewart, Murray |
author_facet | Jani, Divyang Valkov, Eugene Stewart, Murray |
author_sort | Jani, Divyang |
collection | PubMed |
description | The conserved Sac3:Thp1:Sem1:Sus1:Cdc31 (TREX2) complex binds to nuclear pore complexes (NPCs) and, in addition to integrating mRNA nuclear export with preceding steps in the gene expression pathway, facilitates re-positioning of highly regulated actively transcribing genes (such as GAL1) to NPCs. Although TREX2 is thought to bind NPC protein Nup1, defining the precise role of this interaction has been frustrated by the complex pleiotropic phenotype exhibited by nup1Δ strains. To provide a structural framework for understanding the binding of TREX2 to NPCs and its function in the gene expression pathway, we have determined the structure of the Nup1:TREX2 interaction interface and used this information to engineer a Sac3 variant that impairs NPC binding while not compromising TREX2 assembly. This variant inhibited the NPC association of both de-repressed and activated GAL1 and also produced mRNA export and growth defects. These results indicate that the TREX2:Nup1 interaction facilitates the efficient nuclear export of bulk mRNA together with the re-positioning of GAL1 to NPCs that is required for transcriptional control that is mediated by removal of SUMO from repressors by NPC-bound Ulp1. |
format | Online Article Text |
id | pubmed-4041426 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-40414262014-06-11 Structural basis for binding the TREX2 complex to nuclear pores, GAL1 localisation and mRNA export Jani, Divyang Valkov, Eugene Stewart, Murray Nucleic Acids Res Structural Biology The conserved Sac3:Thp1:Sem1:Sus1:Cdc31 (TREX2) complex binds to nuclear pore complexes (NPCs) and, in addition to integrating mRNA nuclear export with preceding steps in the gene expression pathway, facilitates re-positioning of highly regulated actively transcribing genes (such as GAL1) to NPCs. Although TREX2 is thought to bind NPC protein Nup1, defining the precise role of this interaction has been frustrated by the complex pleiotropic phenotype exhibited by nup1Δ strains. To provide a structural framework for understanding the binding of TREX2 to NPCs and its function in the gene expression pathway, we have determined the structure of the Nup1:TREX2 interaction interface and used this information to engineer a Sac3 variant that impairs NPC binding while not compromising TREX2 assembly. This variant inhibited the NPC association of both de-repressed and activated GAL1 and also produced mRNA export and growth defects. These results indicate that the TREX2:Nup1 interaction facilitates the efficient nuclear export of bulk mRNA together with the re-positioning of GAL1 to NPCs that is required for transcriptional control that is mediated by removal of SUMO from repressors by NPC-bound Ulp1. Oxford University Press 2014-06-01 2014-04-04 /pmc/articles/PMC4041426/ /pubmed/24705649 http://dx.doi.org/10.1093/nar/gku252 Text en © The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Structural Biology Jani, Divyang Valkov, Eugene Stewart, Murray Structural basis for binding the TREX2 complex to nuclear pores, GAL1 localisation and mRNA export |
title | Structural basis for binding the TREX2 complex to nuclear pores, GAL1 localisation and mRNA export |
title_full | Structural basis for binding the TREX2 complex to nuclear pores, GAL1 localisation and mRNA export |
title_fullStr | Structural basis for binding the TREX2 complex to nuclear pores, GAL1 localisation and mRNA export |
title_full_unstemmed | Structural basis for binding the TREX2 complex to nuclear pores, GAL1 localisation and mRNA export |
title_short | Structural basis for binding the TREX2 complex to nuclear pores, GAL1 localisation and mRNA export |
title_sort | structural basis for binding the trex2 complex to nuclear pores, gal1 localisation and mrna export |
topic | Structural Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4041426/ https://www.ncbi.nlm.nih.gov/pubmed/24705649 http://dx.doi.org/10.1093/nar/gku252 |
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