Article
Purification and characterization of the human elongator complex.
The Journal of biological chemistry - 25 Jan 2002
Hawkes Nicola A, Otero Gabriel, Winkler G Sebastiaan, Marshall Nick, Dahmus Michael E, Krappmann Daniel, Scheidereit Claus, Thomas Claire L, Schiavo Giampietro, Erdjument-Bromage Hediye, Tempst Paul, Svejstrup Jesper Q
Abstract excerpt
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...
Topics
- Acetyltransferases
- Amino Acid Sequence
- Animals
- Blotting, Western
- Carrier Proteins
- Cell Line
- Cell Nucleus
- Cloning, Molecular
- Dysautonomia, Familial
- HeLa Cells
- Histone Acetyltransferases
- Histones
- Humans