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FACT, PAF-C, and CKII

ABSTRACT: Protein-protein interaction analysis for RNA Polymerase II and its elongation factors including: the PAF Complex, the FACT Complex, casein kinase II, DSIF, and TFIIF. These studies also characterized a number of casein kinase II phosphorylation sites on the subunits of the PAF Complex.

INSTRUMENT(S): LTQ Orbitrap Velos, LTQ Velos

ORGANISM(S): Saccharomyces Cerevisiae (ncbitaxon:4932)

SUBMITTER: Amber L. Mosley

PROVIDER: MSV000079197 | MassIVE | Mon Jul 20 14:57:00 BST 2015

SECONDARY ACCESSION(S): PXD004111

REPOSITORIES: MassIVE

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Quantitative Analysis of Dynamic Protein Interactions during Transcription Reveals a Role for Casein Kinase II in Polymerase-associated Factor (PAF) Complex Phosphorylation and Regulation of Histone H2B Monoubiquitylation.

Bedard Lynn Glowczewski LG Dronamraju Raghuvar R Kerschner Jenny L JL Hunter Gerald O GO Axley Elizabeth DeVlieger ED Boyd Asha K AK Strahl Brian D BD Mosley Amber L AL

The Journal of biological chemistry 20160503 26

Using affinity purification MS approaches, we have identified a novel role for casein kinase II (CKII) in the modification of the polymerase associated factor complex (PAF-C). Our data indicate that the facilitates chromatin transcription complex (FACT) interacts with CKII and may facilitate PAF complex phosphorylation. Posttranslational modification analysis of affinity-isolated PAF-C shows extensive CKII phosphorylation of all five subunits of PAF-C, although CKII subunits were not detected as ...[more]

PMID: 27143358

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