Elongator is a histone H3 and H4 acetyltransferase important for normal histone acetylation levels in vivo Journal Article
| Authors: | Winkler, G. S.; Kristjuhan, A.; Erdjument-Bromage, H.; Tempst, P.; Svejstrup, J. Q. |
| Article Title: | Elongator is a histone H3 and H4 acetyltransferase important for normal histone acetylation levels in vivo |
| Abstract: | The elongating, hyperphosphorylated form of RNA polymerase II is associated with the Elongator complex, which has the histone acetyltransferase (HAT) Elp3 as a subunit. Here we show that, in contrast to the isolated Elp3 subunit, the activity of intact Elongator complex is directed specifically toward the amino-terminal tails of histone H3 and H4, and that Elongator can acetylate both core histones and nucleosomal substrates. The predominant acetylation sites are lysine-14 of histone H3 and lysine-8 of histone H4. The three smallest Elongator subunits-Elp4, Elp5, and Elp6-are required for HAT activity, and Elongator binds to both naked and nucleosomal DNA. By using chromatin immunoprecipitation, we show that the levels of multiply acetylated histone H3 and H4 in chromatin are decreased in vivo in yeast cells lacking ELP3. |
| Keywords: | gene deletion; nonhuman; enzyme phosphorylation; protein purification; saccharomyces cerevisiae; chromatin; histone h3; substrate specificity; immunoprecipitation; yeast; saccharomyces cerevisiae proteins; nucleic acid conformation; protein subunits; rna polymerase ii; histones; enzyme assay; lysine; acetyltransferases; electrophoretic mobility; acetylation; macromolecular substances; dna fragment; tritium; plasmid dna; dna, fungal; nucleosomes; histone h4; synthetic peptide; saccharomyces; ribosome dna; acetyl coenzyme a; histone acetyltransferase; histone acetyltransferases; holoenzymes; precipitin tests; priority journal; article |
| Journal Title: | Proceedings of the National Academy of Sciences of the United States of America |
| Volume: | 99 |
| Issue: | 6 |
| ISSN: | 0027-8424 |
| Publisher: | National Academy of Sciences |
| Date Published: | 2002-03-19 |
| Start Page: | 3517 |
| End Page: | 3522 |
| Language: | English |
| DOI: | 10.1073/pnas.022042899 |
| PUBMED: | 11904415 |
| PROVIDER: | scopus |
| PMCID: | PMC122555 |
| DOI/URL: | |
| Notes: | Export Date: 14 November 2014 -- Source: Scopus |
