CK2 forms a stable complex with TFIII3 and activates RNA polymerase III transcription in human cells

Johnston, I. M., Allison, S. J., Morton, J. P., Schramm, L., Scott, P. H., White, R. J. (June 2002) CK2 forms a stable complex with TFIII3 and activates RNA polymerase III transcription in human cells. Molecular and Cellular Biology, 22 (11). pp. 3757-3768. ISSN 0270-7306

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URL: http://www.ncbi.nlm.nih.gov/pubmed/11997511
DOI: 10.1128/MCB.22.11.3757-3768.2002

Abstract

CK2 is a highly conserved protein kinase with growth-promoting and oncogenic properties. It is known to activate RNA polymerase III (PolIII) transcription in Saccharomyces cerevisiae and is shown here to also exert a potent effect on PolIII in mammalian cells. Peptide and chemical inhibitors of CK2 block PolIII transcription in human cell extracts. Furthermore, PolIII transcription in mammalian fibroblasts is decreased significantly when CK2 activity is compromised by chemical inhibitors, antisense oligonucleotides, or kinase-inactive mutants. Coimmunoprecipitation and cofractionation show that endogenous human CK2 associates stably and specifically with the TATA-binding protein-containing factor TFIIIB, which brings PolIII to the initiation site of all class III genes. Serum stimulates TFIIIB phosphorylation in vivo, an effect that is diminished by inhibitors of CK2. Binding to TFIIIC2 recruits TFIIIB to most PolIII promoters; this interaction is compromised specifically by CK2 inhibitors. The data suggest that CK2 stimulates PolIII transcription by binding and phosphorylating TFIIIB and facilitating its recruitment by TFIIIC2. CK2 also activates PolI transcription in mammals and may therefore provide a mechanism to coregulate the output of PolI and PolIII. CK2 provides a rare example of an endogenous activity that operates on the PolIII system in both mammals and yeasts. Such evolutionary conservation suggests that this control may be of fundamental importance.

Item Type: Paper
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > transcription
bioinformatics > genomics and proteomics > genetics & nucleic acid processing
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > RNA polymerase
organism description > animal > mammal > primates > hominids > human
CSHL Authors:
Communities: CSHL labs > Hernandez lab
Depositing User: Matt Covey
Date: June 2002
Date Deposited: 08 Jan 2014 17:02
Last Modified: 08 Jan 2014 17:02
PMCID: PMC133823
Related URLs:
URI: http://repository.cshl.edu/id/eprint/28726

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