| Abstract: |
The Srb8, -9, -10, and -11 proteins of yeast have been isolated as a discrete, stoichiometric complex. The isolated complex phosphorylates the C-terminal domain (CTD) of the largest subunit of RNA polymerase II at serines 2 and 5. In addition to the previously reported human homologs of Srb10 and 11, we have identified TRAP230/ARC240 and TRAP240/ARC250 as the human homologs of Srb8 and Srb9, showing the entire Srb8/9/ 10/11 complex is conserved from yeast to humans. |
| Keywords: |
protein phosphorylation; unclassified drug; mutation; nonhuman; proteins; protein analysis; animals; serine; carboxy terminal sequence; transcription, genetic; phosphorylation; time factors; transcription factors; transcription regulation; amino acid sequence; molecular sequence data; sequence homology, amino acid; immunoglobulin g; saccharomyces cerevisiae; protein structure, tertiary; yeast; saccharomyces cerevisiae proteins; cyclin-dependent kinases; enzyme subunit; biochemistry; rna polymerase ii; electrophoresis, polyacrylamide gel; regulator protein; stoichiometry; transcription factor tfiih; databases; tata-binding protein associated factors; transcription factor tfiid; protein srb10; protein srb11; transcription factors, tfii; humans; priority journal; article; stoichiometric complex; protein srb8; protein srb9
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