Elongator, a Multisubunit Component of a Novel RNA Polymerase II Holoenzyme for Transcriptional Elongation
| Autor: | Hediye Erdjument-Bromage, Paul Tempst, Jesper Q. Svejstrup, Annette M.G. Dirac, Jane Fellows, Yang Li, Claes M. Gustafsson, Gabriel Otero, Therese de Bizemont |
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| Rok vydání: | 1999 |
| Předmět: |
Transcriptional Activation
Transcription Genetic Protein subunit RNA polymerase II Saccharomyces cerevisiae Biology ELP3 Fungal Proteins Mediator Transcription (biology) Cloning Molecular Phosphorylation RNA polymerase II holoenzyme Molecular Biology Regulation of gene expression Fungal protein Cell Biology Molecular biology Cell biology Phenotype Gene Expression Regulation biology.protein RNA Polymerase II Transcription Factors General Transcriptional Elongation Factors Cell Division Protein Binding Transcription Factors |
| Zdroj: | Molecular Cell. 3(1):109-118 |
| ISSN: | 1097-2765 |
| DOI: | 10.1016/s1097-2765(00)80179-3 |
| Popis: | The form of RNA polymerase II (RNAPII) engaged in transcriptional elongation was isolated. Elongating RNAPII was associated with a novel multisubunit complex, termed elongator, whose stable interaction was dependent on a hyperphosphorylated state of the RNAPII carboxy-terminal domain (CTD). A free form of elongator was also isolated, demonstrating the discrete nature of the complex, and free elongator could bind directly to RNAPII. The gene encoding the largest subunit of elongator, ELP1, was cloned. Phenotypes of yeast elp1 delta cells demonstrated an involvement of elongator in transcriptional elongation as well as activation in vivo. Our data indicate that the transition from transcriptional initiation to elongation involves an exchange of the multiprotein mediator complex for elongator in a reaction coupled to CTD hyperphosphorylation. |
| Databáze: | OpenAIRE |
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