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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. | LitMetric

AI Article Synopsis

  • Researchers discovered a new function of casein kinase II (CKII) in modifying the polymerase associated factor complex (PAF-C) through their affinity purification mass spectrometry approaches.
  • The study revealed that the FACT complex interacts with CKII and is involved in the phosphorylation of PAF-C, which is crucial for transcription regulation.
  • Additionally, experiments showed that reduced CKII function leads to lower levels of a specific histone modification, indicating CKII's important role in RNA polymerase II transcription regulation via PAF-C.

Article Abstract

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 interacting partners. Consistent with this, recombinant CKII or FACT-associated CKII isolated from cells can phosphorylate PAF-C in vitro, whereas no intrinsic kinase activity was detected in PAF-C samples. Significantly, PAF-C purifications combined with stable isotope labeling in cells (SILAC) quantitation for PAF-C phosphorylation from wild-type and CKII temperature-sensitive strains (cka1Δ cka2-8) showed that PAF-C phosphorylation at consensus CKII sites is significantly reduced in cka1Δ cka2-8 strains. Consistent with a role of CKII in FACT and PAF-C function, we show that decreased CKII function in vivo results in decreased levels of histone H2B lysine 123 monoubiquitylation, a modification dependent on FACT and PAF-C. Taken together, our results define a coordinated role of CKII and FACT in the regulation of RNA polymerase II transcription through chromatin via phosphorylation of PAF-C.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4919428PMC
http://dx.doi.org/10.1074/jbc.M116.727735DOI Listing

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