RNA polymerase II termination involves CTD tyrosine dephosphorylation by CPF subunit Glc7
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ABSTRACT: 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].
ORGANISM(S): Saccharomyces cerevisiae
SUBMITTER: Michael Lidschreiber
PROVIDER: E-MTAB-1528 | biostudies-arrayexpress |
REPOSITORIES: biostudies-arrayexpress
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