Structural basis of eukaryotic gene transcription.
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 approximately 3 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.
Boeger
Hinrich
H
Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Bushnell
David A
DA
Davis
Ralph
R
Griesenbeck
Joachim
J
Lorch
Yahli
Y
Strattan
J Seth
JS
Westover
Kenneth D
KD
Kornberg
Roger D
RD
D018360:Crystallography, X-Ray; D005057:Eukaryotic Cells / Q000378:metabolism*; D015394:Molecular Structure; D009707:Nucleosomes / Q000737:chemistry*; D011401:Promoter Regions, Genetic / Q000235:genetics*; D012319:RNA Polymerase II / Q000737:chemistry*; D014158:Transcription, Genetic
D009707:Nucleosomes; D012319:RNA Polymerase II