RNA polymerase II elongator holoenzyme is composed of two discrete subcomplexes.
Elongator is a histone acetyltransferase complex that associates with the elongating form of RNA polymerase II. We purified Elongator to virtual homogeneity via a rapid three-step procedure based largely on affinity chromatography. The purified factor, holo-Elongator, is a labile six-subunit factor composed of two discrete subcomplexes: one comprised of the ... previously identified Elp1, Elp2, and Elp3 proteins and another comprised of three novel polypeptides, termed Elp4, Elp5, and Elp6. Disruption of the yeast genes encoding the new Elongator proteins confers phenotypes indistinguishable from those previously described for the other elp mutants, and concomitant disruption of genes encoding proteins in either subcomplex does not confer new phenotypes. Taken together, our results indicate that holo-Elongator is a functional entity in vitro as well as in vivo. Metazoan homologues of Elp1 and Elp3 have previously been reported. We cloned the human homologue of yeast ELP4 and show that this gene is ubiquitously expressed in human tissues.
Mesh Terms:
Acetyltransferases, Amino Acid Sequence, Animals, Caenorhabditis elegans, Cloning, Molecular, Conserved Sequence, Drosophila melanogaster, Histone Acetyltransferases, Humans, Macromolecular Substances, Mice, Molecular Sequence Data, Peptide Fragments, Phenotype, Protein Subunits, RNA Polymerase II, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Schizosaccharomyces, Sequence Alignment, Sequence Homology, Amino Acid, Transcription, Genetic
Acetyltransferases, Amino Acid Sequence, Animals, Caenorhabditis elegans, Cloning, Molecular, Conserved Sequence, Drosophila melanogaster, Histone Acetyltransferases, Humans, Macromolecular Substances, Mice, Molecular Sequence Data, Peptide Fragments, Phenotype, Protein Subunits, RNA Polymerase II, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Schizosaccharomyces, Sequence Alignment, Sequence Homology, Amino Acid, Transcription, Genetic
J. Biol. Chem.
Date: Aug. 31, 2001
PubMed ID: 11435442
View in: Pubmed Google Scholar
Download Curated Data For This Publication
16066
Switch View:
- Interactions 8