Transcriptomics

Dataset Information

296

ChIP-chip by array of budding yeast to study RNA polymerase II termination using anti-Rpb3 and anti-TyrY1P antibodies


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].

INSTRUMENT(S): 418 [Affymetrix]

ORGANISM(S): Saccharomyces cerevisiae  

SUBMITTER: Michael Lidschreiber  

PROVIDER: E-MTAB-1528 | ArrayExpress | 2013-12-16

REPOSITORIES: ArrayExpress

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Publications

RNA polymerase II termination involves C-terminal-domain tyrosine dephosphorylation by CPF subunit Glc7.

Schreieck Amelie A   Easter Ashley D AD   Etzold Stefanie S   Wiederhold Katrin K   Lidschreiber Michael M   Cramer Patrick P   Passmore Lori A LA  

Nature structural & molecular biology 20140112 2


At the 3' ends of protein-coding genes, RNA polymerase (Pol) II is dephosphorylated at tyrosine residues (Tyr1) of its C-terminal domain (CTD). In addition, the associated cleavage-and-polyadenylation factor (CPF) cleaves the transcript and adds a poly(a) tail. Whether these events are coordinated and how they lead to transcription termination remains poorly understood. Here we show that CPF from Saccharomyces cerevisiae is a Pol II-CTD phosphatase and that the CPF subunit Glc7 dephosphorylates  ...[more]

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