Recruitment of TREX to the Transcription Machinery by Its Direct Binding to the Phospho-CTD of RNA Polymerase II

Dominik M. Meinel, Cornelia Burkert-Kautzsch, Anja Kieser, Eoghan O'Duibhir, Matthias Siebert, Andreas Mayer, Patrick Cramer, Johannes Söding, Frank C.P. Holstege, Katja Sträßer

Research output: Contribution to journalArticlepeer-review

55 Citations (Scopus)

Abstract

Messenger RNA (mRNA) synthesis and export are tightly linked, but the molecular mechanisms of this coupling are largely unknown. In Saccharomyces cerevisiae, the conserved TREX complex couples <underline>tr</underline>anscription to mRNA <underline>ex</underline>port and mediates mRNP formation. Here, we show that TREX is recruited to the transcription machinery by direct interaction of its subcomplex THO with the serine 2-serine 5 (S2/S5) diphosphorylated CTD of RNA polymerase II. S2 and/or tyrosine 1 (Y1) phosphorylation of the CTD is required for TREX occupancy in vivo, establishing a second interaction platform necessary for TREX recruitment in addition to RNA. Genome-wide analyses show that the occupancy of THO and the TREX components Sub2 and Yra1 increases from the 5′ to the 3′ end of the gene in accordance with the CTD S2 phosphorylation pattern. Importantly, in a mutant strain, in which TREX is recruited to genes but does not increase towards the 3′ end, the expression of long transcripts is specifically impaired. Thus, we show for the first time that a 5′-3′ increase of a protein complex is essential for correct expression of the genome. In summary, we provide insight into how the phospho-code of the CTD directs mRNP formation and export through TREX recruitment.

Original languageEnglish
Article numbere1003914
JournalPLoS Genetics
Volume9
Issue number11
DOIs
Publication statusPublished - Nov 2013
Externally publishedYes

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