E-MTAB-1528 - ChIP-chip by array of budding yeast to study RNA polymerase II termination using anti-Rpb3 and anti-TyrY1P antibodies
Last updated on 5 December 2013, released on 16 December 2013
At the 3'-ends of genes, RNA polymerase (Pol) II is dephosphorylated at tyrosine 1 residues of its C-terminal domain (CTD), resulting in recruitment of transcription termination factors. We show that the multisubunit cleavage and polyadenylation factor (CPF) is a Pol II CTD phosphatase and its Glc7 subunit is required for Tyr1 dephosphorylation at the poly-adenylation site and Pol II termination in vivo. ChIP-chip was performed to examine the effect of Glc7 nuclear depletion on genome-wide Pol II occupancy [using ?-Rpb3 (1Y26, cat. no. W0012, neoclone) antibody] and CTD tyrosine 1 phosphorylation levels [using ?-TyrY1P (3D12, D. Eick) antibody].
ChIP-chip by array, binding site identification, cellular process design, in vivo design
RNA polymerase II termination involves C-terminal-domain tyrosine dephosphorylation by CPF subunit Glc7. Schreieck A, Easter AD, Etzold S, Wiederhold K, Lidschreiber M, Cramer P, Passmore LA. :175-179 (2014), Europe PMC 24413056
RNA polymerase II termination involves CTD tyrosine dephosphorylation by CPF subunit Glc7.