On the subunit composition, stoichiometry, and phosphorylation of the yeast transcription factor TFIIIC/tau.

Saccharomyces cerevisiae transcription factor IIIC/tau is a multisubunit DNA-binding protein that plays key roles in tRNA and 5 S rRNA gene activation. Subunit composition, stoichiometry, and in vivo phosphorylation of TFIIIC/tau factor were investigated using factor prepared from strains carrying modified forms of TFC1, the gene encoding the 95-kDa TFIIIC/tau ...
subunit (tau 95). Using an epitope-tagged TFC1 as well as a TFC1-lacZ fusion, TFIIIC was shown to contain a single 95-kDa subunit, which was localized by electron microscopy into tau A, the A block-binding domain of TFIIIC/tau. Three 35S-labeled polypeptides (at 138, 131, and 91 kDa) coimmunoprecipitated with a tau 95-beta-galactosidase fusion protein. The coprecipitation of the 91-kDa polypeptide makes it a likely subunit of the factor. Immunoprecipitation from 32P-labeled extracts revealed that three of the subunits (138, 131, and 95 kDa), but not the 91-kDa component, are phosphorylated in vivo.
Mesh Terms:
Base Sequence, Binding Sites, Electrophoresis, Polyacrylamide Gel, Epitopes, Genes, Fungal, Kinetics, Macromolecular Substances, Microscopy, Electron, Molecular Sequence Data, Molecular Weight, Mutagenesis, Site-Directed, Oligodeoxyribonucleotides, Phosphorus Radioisotopes, Phosphorylation, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Sulfur Radioisotopes, Transcription Factors, Transcription Factors, TFIII, Transcription, Genetic, beta-Galactosidase
J. Biol. Chem.
Date: Aug. 25, 1993
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