Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10873950 | FEBS Letters | 2005 | 5 Pages |
Abstract
An RNA polymerase II promoter has been isolated in transcriptionally activated and repressed states. Topological and nuclease digestion analyses have revealed a dynamic equilibrium between nucleosome removal and reassembly upon transcriptional activation, and have further shown that nucleosomes are removed by eviction of histone octamers rather than by sliding. The promoter, once exposed, assembles with RNA polymerase II, general transcription factors, and Mediator in a â¼3 MDa transcription initiation complex. X-ray crystallography has revealed the structure of RNA polymerase II, in the act of transcription, at atomic resolution. Extension of this analysis has shown how nucleotides undergo selection, polymerization, and eventual release from the transcribing complex. X-ray and electron crystallography have led to a picture of the entire transcription initiation complex, elucidating the mechanisms of promoter recognition, DNA unwinding, abortive initiation, and promoter escape.
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Hinrich Boeger, David A. Bushnell, Ralph Davis, Joachim Griesenbeck, Yahli Lorch, J. Seth Strattan, Kenneth D. Westover, Roger D. Kornberg,