TREX is a conserved complex coupling transcription with messenger RNA export

@article{Strer2002TREXIA,
  title={TREX is a conserved complex coupling transcription with messenger RNA export},
  author={Katja Str{\"a}{\ss}er and Seiji Masuda and Paul B. Mason and Jens Pfannstiel and Marisa Oppizzi and Susana Rodr{\'i}guez-Navarro and Ana G Rond{\'o}n and Andr{\'e}s Aguilera and Kevin Struhl and Robin Reed and Ed Hurt},
  journal={Nature},
  year={2002},
  volume={417},
  pages={304-308}
}
The essential yeast proteins Yra1 and Sub2 are messenger RNA export factors that have conserved counterparts in metazoans, designated Aly and UAP56, respectively. These factors couple the machineries that function in splicing and export of mRNA. Here we show that both Yra1 and Sub2 are stoichiometrically associated with the heterotetrameric THO complex, which functions in transcription in yeast. We also show that Sub2 and Yra1 interact genetically with all four components of the THO complex… 
Transcription, Splicing and mRNA Export Are Coupled Events
The machineries involved in gene expression are highly conserved from yeast to metazoans. However, a fundamental difference between these organisms is that most yeast genes lack introns whereas the
Expression of the essential mRNA export factor Yra1p is autoregulated by a splicing-dependent mechanism.
TLDR
It is shown here that overexpression of the intron-containing gene results in increased levels of unspliced pre-mRNA but normal levels of Yra1 protein; conversely, expression of the cDNA results inIncreased levels of protein and accumulation of nuclear poly(A)+ RNA.
The yeast THO complex and mRNA export factors link RNA metabolism with transcription and genome instability
TLDR
A functional link between the processes of elongation and metabolism of nascent mRNA mediated by THO and mRNA export proteins, which have important consequences for the maintenance of genome stability are indicated.
The yeast THO complex forms a 5-subunit assembly that directly interacts with active chromatin
TLDR
The cellular role of THO is reviewed, which is shown to be composed of five subunits with Tex1 being also an integral part of the complex, with which it forms the TRanscription and EXport complex (TREX).
Mud2 functions in transcription by recruiting the Prp19 and TREX complexes to transcribed genes
TLDR
Mud2 is classified as a novel transcription factor that is necessary for the recruitment of mRNA-binding proteins to the transcription machinery and is a multifunctional protein important for transcription, splicing and most likely also mRNP packaging.
The RNA binding protein Mip6, a novel cellular partner of Mex67 export factor with implications in mRNA export
Nuclear export of messenger ribonucleic acid (mRNA) is a complex and essential process for a correct gene expression in all eukaryotic cells. The export of mRNA through the nuclear pore complex
Recruitment of TREX to the Transcription Machinery by Its Direct Binding to the Phospho-CTD of RNA Polymerase II
TLDR
In insight into how the phospho-code of the CTD directs mRNP formation and export through TREX recruitment is provided, it is shown for the first time that a 5′-3′ increase of a protein complex is essential for correct expression of the genome.
Biochemical analysis of TREX complex recruitment to intronless and intron‐containing yeast genes
TLDR
These experiments support a model in which TREX is recruited via the transcription machinery and then Yra1p and Sub2p are transferred to the nascent RNA, and on some intron‐containing genes, retention and/or transfer of Yra 1p andsub2p to nascent RNA are inhibited.
Structure of the human core transcription-export complex reveals a hub for multivalent interactions
TLDR
The cryo-electron microscopy structure of the human THO–UAP56/DDX39B complex is reported, suggesting a conserved model for TREX complex function that depends on multivalent interactions between proteins and mRNA.
URH49 exports mRNA by remodeling complex formation and mediating the NXF1-dependent pathway.
TLDR
An mRNA export model that the mRNA selectivity depends on the Apo-form TREX/AREX complex, which is remodeled to the highly similar ATP-form complex upon ATP loading, and integrated to NXF1 is proposed.
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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