A Novel Histone Acetyltransferase Is an Integral Subunit of Elongating RNA Polymerase II Holoenzyme
| Autor: | Jane Fellows, Paul Tempst, Birgitte Ø. Wittschieben, Reiko Ohba, Yang Li, C. David Allis, Gabriel Otero, Hediye Erdjument-Bromage, Jesper Q. Svejstrup, Therese de Bizemont |
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| Rok vydání: | 1999 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Specificity factor Molecular Sequence Data RNA polymerase II Saccharomyces cerevisiae ELP3 Fungal Proteins Acetyltransferases Transcription (biology) Amino Acid Sequence Cloning Molecular Molecular Biology RNA polymerase II holoenzyme Histone Acetyltransferases biology Cell Biology Histone acetyltransferase Molecular biology Chromatin Recombinant Proteins Cell biology Phenotype biology.protein RNA Polymerase II Transcription factor II D Sequence Alignment Gene Deletion |
| Zdroj: | Molecular Cell. 4:123-128 |
| ISSN: | 1097-2765 |
| DOI: | 10.1016/s1097-2765(00)80194-x |
| Popis: | The elongator complex is a major component of the RNA polymerase II (RNAPII) holoenzyme responsible for transcriptional elongation in yeast. Here we identify Elp3, the 60-kilodalton subunit of elongator/RNAPII holoenzyme, as a highly conserved histone acetyltransferase (HAT) capable of acetylating core histones in vitro. In vivo, ELP3 gene deletion confers typical elp phenotypes such as slow growth adaptation, slow gene activation, and temperature sensitivity. These results suggest a role for a novel, tightly RNAPII-associated HAT in transcription of DNA packaged in chromatin. |
| Databáze: | OpenAIRE |
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