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Purification and characterization of the human Elongator complex

Item Type:Article
Title:Purification and characterization of the human Elongator complex
Creators Name:Hawkes, N.A. and Otero, G. and Winkler, G.S. and Marshall, N. and Dahmus, M.E. and Krappmann, D. and Scheidereit, C. and Thomas, C.L. and Schiavo, G. and Erdjument-Bromage, H. and Tempst, P. and Svejstrup, J.Q.
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:Acetyltransferases, Amino Acid Sequence, Amino Acid Sequence Homology, Carrier Proteins, Cell Line, Cell Nucleus, Familial Dysautonomia, Genetic Transcription, Hela Cells, Histone Acetyltransferases, Histones, Insects, Intracellular Signaling Peptides and Proteins, Molecular Cloning, Molecular Sequence Data, Mutation, Protein Binding, RNA Polymerase II, Saccharomyces cerevisiae Proteins, Tertiary Protein Structure, Western Blotting, Animals
Source:Journal of Biological Chemistry
Publisher:American Society for Biochemistry and Molecular Biology
Page Range:3047-3052
Date:1 January 2002
Official Publication:https://doi.org/10.1074/jbc.M110445200
PubMed:View item in PubMed

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