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Structural basis of eukaryotic gene transcription
Author(s) -
Boeger Hinrich,
Bushnell David A.,
Davis Ralph,
Griesenbeck Joachim,
Lorch Yahli,
Strattan J. Seth,
Westover Kenneth D.,
Kornberg Roger D.
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.11.027
Subject(s) - rna polymerase ii , transcription (linguistics) , transcription factor ii f , general transcription factor , transcription bubble , transcription factor ii d , rna polymerase ii holoenzyme , nucleosome , microbiology and biotechnology , abortive initiation , biology , transcription factor ii e , promoter , transcription preinitiation complex , rna polymerase , eukaryotic transcription , rna polymerase i , polymerase , transcription factor ii b , histone , rna , dna , gene , genetics , gene expression , linguistics , philosophy
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 ∼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.