STRUCTURAL INSIGHTS INTO RECRUITMENT AND DISSOCIATION OF RNA POLYMEARSE II TERMINATION FACTORS

K. Kubíček^1,2, H. Černá¹, C. Hofr³, R. Štefl¹

¹National Centre for Biomolecular Research

²Dept. of Condensed Matter Physics

³Dept. of Experimental Biology

Masaryk University, Faculty of Science, 625 00 Brno, Czech Republic

karelk@chemi.muni.cz

RNA Polymerase II recruits many accessory factors via its C-terminal domain (CTD). During the transcription cycle, CTD is dynamically phosphorylated and dephosphorylated that promote binding of required protein factors. Transcription termination occurs either with CTD phosphorylated at Ser2 or Ser5 via poly(A)-dependent or independent termination pathways, respectively. Using NMR and other biophysical methods, we aim at understanding of structural determinants that define binding and dissociation of accessory protein factors to specifically phosphorylated CTD species