» Articles » PMID: 14769921

Cotranscriptional Recruitment of the Serine-arginine-rich (SR)-like Proteins Gbp2 and Hrb1 to Nascent MRNA Via the TREX Complex

Overview
Specialty Science
Date 2004 Feb 11
PMID 14769921
Citations 81
Authors
Affiliations
Soon will be listed here.
Abstract

The TREX (transcription/export) complex couples transcription elongation to the nuclear export of mRNAs. In this article, we show that the poly(A)(+) RNA-binding proteins Gbp2 and Hrb1, which resemble the serine-arginine-rich (SR) family of splicing factors found in higher eukaryotes, are specifically associated with the yeast TREX complex. We also show that Gbp2 and Hrb1 interact with Ctk1, a kinase that phosphorylates the C-terminal domain of RNA polymerase II during transcription elongation. Consistent with these findings, Gbp2 and Hrb1 associate with actively transcribed genes throughout their entire lengths. By using an RNA immunoprecipitation assay, we show that Gbp2 and Hrb1 also are bound to transcripts that are derived from these genes. We conclude that recruitment of the SR-like proteins Gbp2 and Hrb1 to mRNA occurs cotranscriptionally by means of association with the TREX complex and/or Ctk1.

Citing Articles

Structures and mRNP remodeling mechanism of the TREX-2 complex.

Xie Y, Clarke B, Xie D, Mei M, Bhat P, Hill P Structure. 2025; 33(3):566-582.e6.

PMID: 39862860 PMC: 11890942. DOI: 10.1016/j.str.2024.12.019.


Defenders of the Transcriptome: Guard Protein-Mediated mRNA Quality Control in .

Querl L, Krebber H Int J Mol Sci. 2024; 25(19).

PMID: 39408571 PMC: 11476243. DOI: 10.3390/ijms251910241.


Cryo-EM structure of the CBC-ALYREF complex.

Clarke B, Angelos A, Mei M, Hill P, Xie Y, Ren Y Elife. 2024; 12.

PMID: 39282949 PMC: 11405014. DOI: 10.7554/eLife.91432.


PCID2 dysregulates transcription and viral RNA processing to promote HIV-1 latency.

Crespo R, Ne E, Reinders J, Meier J, Li C, Jansen S iScience. 2024; 27(3):109152.

PMID: 38384833 PMC: 10879814. DOI: 10.1016/j.isci.2024.109152.


Tho2 is critical for the recruitment of Rrp6 to chromatin in response to perturbed mRNP biogenesis.

Beauvais V, Moreau K, Zunar B, Hervouet-Coste N, Novacic A, Le Dantec A RNA. 2023; 30(1):89-98.

PMID: 37914399 PMC: 10726162. DOI: 10.1261/rna.079707.123.


References
1.
Rondon A, Jimeno S, Garcia-Rubio M, Aguilera A . Molecular evidence that the eukaryotic THO/TREX complex is required for efficient transcription elongation. J Biol Chem. 2003; 278(40):39037-43. DOI: 10.1074/jbc.M305718200. View

2.
Strasser K, Masuda S, Mason P, Pfannstiel J, Oppizzi M, Rodriguez-Navarro S . TREX is a conserved complex coupling transcription with messenger RNA export. Nature. 2002; 417(6886):304-8. DOI: 10.1038/nature746. View

3.
Lee M, Henry M, Silver P . A protein that shuttles between the nucleus and the cytoplasm is an important mediator of RNA export. Genes Dev. 1996; 10(10):1233-46. DOI: 10.1101/gad.10.10.1233. View

4.
Lee J, Greenleaf A . Modulation of RNA polymerase II elongation efficiency by C-terminal heptapeptide repeat domain kinase I. J Biol Chem. 1997; 272(17):10990-3. DOI: 10.1074/jbc.272.17.10990. View

5.
Rigaut G, Shevchenko A, Rutz B, Wilm M, Mann M, Seraphin B . A generic protein purification method for protein complex characterization and proteome exploration. Nat Biotechnol. 1999; 17(10):1030-2. DOI: 10.1038/13732. View