| Abstract: |
Human Elongator complex was purified to virtual homogeneity from HeLa cell extracts. The purified factor can exist in two forms: a six-subunit complex, holo-Elongator, which has histone acetyltransferase activity directed against histone H3 and H4, and a three-subunit core form, which does not have histone acetyltransferase activity despite containing the catalytic Elp3 subunit. Elongator is a component of early elongation complexes formed in HeLa nuclear extracts and can interact directly with RNA polymerase II in solution. Several human homologues of the yeast Elongator subunits were identified as subunits of the human Elongator complex, including StIP1 (STAT-interacting protein 1) and IKAP (IKK complex-associated protein). Mutations in IKAP can result in the severe human disorder familial dysautonomia, raising the possibility that this disease might be due to compromised Elongator function and therefore could be a transcription disorder. |
| Keywords: |
controlled study; unclassified drug; human cell; mutation; nonhuman; protein analysis; animal cell; animals; familial disease; cell line; protein; protein binding; genetic transcription; transcription, genetic; hela cell; hela cells; animalia; rna; cloning, molecular; blotting, western; amino acid sequence; molecular sequence data; sequence homology, amino acid; protein purification; intracellular signaling peptides and proteins; histone h3; carrier proteins; protein structure, tertiary; cell nucleus; yeast; saccharomyces cerevisiae proteins; catalysis; rna polymerase ii; histones; enzymes; acetyltransferases; dysautonomia; elongation factor; histone h4; cells; insects; purification; histone acetyltransferase; histone acetyltransferases; dysautonomia, familial; humans; human; priority journal; article; human elongator complex; ikk complex associated protein; stat interacting protein 1
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