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Rpb4/7 heterodimer regulates RNAPII phosphorylation

AutorAllepuz-Fuster, Paula; Martínez-Fernández, Verónica; Garrido-Godino, Ana I.; Navarro, Francisco; Calvo, Olga
Fecha de publicación2014
CitaciónEMBO Conferences: Gene Transcription in Yeast: From regulatory networks to mechanisms (2014)
ResumenThe 12-subunit RNA polymerase II enzyme in eukaryotic cells is essential for transcription of protein-coding genes. The Rpb4 and Rpb7 subunits bind to each other forming a complex in archaebacteria and in eukaryotic cells, and display some unique features that distinguish them from the remaining subunits. In S. cerevisiae, the Rpb4/7 heterodimer can dissociate from the rest of the holoenzyme. These subunits are important for transcription initiation, elongation and, in particular, Rpb4 contributes to contranscriptional recruitment of 3’-end processing factors. However, recent evidences suggests that they are also involved in DNA repair, mRNA export and decay, as well as translation. Additionally, several facts suggest that Rpb4/7 may play a role on RNAPII phosphorylation: 1) The close proximity of the Rpb4/7 heterodimer to the CTD of the Rpb1. 2) The in vitro concerted interaction of Rpb4 and the CTD phosphatase, Fcp1, in S. pombe, suggesting that Rpb4 may play an important role in the assembly of Fcp1 into the RNAPII complex and thus, also in dephosphorylation. 3) The Rpb4-Fcp1 interaction is also conserved in Drosophila; and 4) in Saccharomyces cerevisiae, Rpb7 genetically interacts with the propyl isomerase Ess1, also involved in CTD phosphorylation regulation. Here, we present genetic and biochemical data showing that effectively Rpb4/7 subcomplex is important for RNAPII dephosphorylation in S. cerevisiae, regulating several CTD modifying enzymes.
DescripciónPóster presentado a la EMBO Conferences: Gene Transcription in Yeast: From regulatory networks to mechanisms, celebrada en Sant Feliu de Guixols (España) del 14 al 19 de junio de 2014.
URIhttp://hdl.handle.net/10261/117026
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