RNA polymerase II elongator holoenzyme is composed of two discrete subcomplexes Journal Article
| Authors: | Sebastiaan Winkler, G.; Petrakis, T. G.; Ethelberg, S.; Tokunaga, M.; Erdjument-Bromage, H.; Tempst, P.; Svejstrup, J. Q. |
| Article Title: | RNA polymerase II elongator holoenzyme is composed of two discrete subcomplexes |
| Abstract: | 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. |
| Keywords: | unclassified drug; genetics; nonhuman; molecular genetics; mouse; phenotype; animal; metabolism; animals; mice; genes; protein protein interaction; gene product; genetic transcription; transcription, genetic; rna; molecular cloning; cloning, molecular; chemistry; amino acid sequence; conserved sequence; molecular sequence data; sequence homology, amino acid; saccharomyces cerevisiae; sequence alignment; gene disruption; nucleotide sequence; peptide fragments; recombinant proteins; peptide fragment; recombinant protein; caenorhabditis elegans; drosophila melanogaster; yeast; saccharomyces cerevisiae proteins; protein subunit; saccharomyces cerevisiae protein; protein subunits; sequence homology; enzyme subunit; biochemistry; isolation and purification; rna polymerase ii; enzymes; acyltransferase; acetyltransferases; tissue; schizosaccharomyces; mutant; macromolecule; macromolecular substances; metazoa; polypeptides; polypeptide; cloning; affinity chromatography; holoenzyme; histone acetyltransferase; histone acetyltransferases; humans; human; priority journal; article; protein elp1; genes encoding; protein elp2; protein elp3; protein elp4; protein elp5; protein elp6 |
| Journal Title: | Journal of Biological Chemistry |
| Volume: | 276 |
| Issue: | 35 |
| ISSN: | 0021-9258 |
| Publisher: | American Society for Biochemistry and Molecular Biology |
| Date Published: | 2001-08-31 |
| Start Page: | 32743 |
| End Page: | 32749 |
| Language: | English |
| DOI: | 10.1074/jbc.M105303200 |
| PUBMED: | 11435442 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Export Date: 21 May 2015 -- Source: Scopus |
