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  Structure–function studies of the RNA polymerase II elongation complex.

Brueckner, F., Armache, K. J., Cheung, A., Damsma, G. E., Kettenberger, H., Lehmann, E., et al. (2009). Structure–function studies of the RNA polymerase II elongation complex. Acta Crystallographica Section D: Biological Crystallography, 65(2), 112-120. doi:10.1107/S0907444908039875.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0015-7B63-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-C5CB-9
Genre: Journal Article

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1935914.pdf (Publisher version), 3MB
 
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 Creators:
Brueckner, F., Author
Armache, K. J., Author
Cheung, A., Author
Damsma, G. E., Author
Kettenberger, H., Author
Lehmann, E., Author
Sydow, J., Author
Cramer, P.1, Author              
Affiliations:
1Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1863498              

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Free keywords: nucleic acids; transcription elongation; RNA polymerase II; nucleotide-addition cycle; translocation; transcription factor IIS; DNA-damage recognition; RNA-dependent RNA polymerase activity
 Abstract: RNA polymerase II (Pol II) is the eukaryotic enzyme that is responsible for transcribing all protein-coding genes into messenger RNA (mRNA). The mRNA-transcription cycle can be divided into three stages: initiation, elongation and termination. During elongation, Pol II moves along a DNA template and synthesizes a complementary RNA chain in a processive manner. X-ray structural analysis has proved to be a potent tool for elucidating the mechanism of Pol II elongation. Crystallographic snapshots of different functional states of the Pol II elongation complex (EC) have elucidated mechanistic details of nucleotide addition and Pol II translocation. Further structural studies in combination with in vitro transcription experiments led to a mechanistic understanding of various additional features of the EC, including its inhibition by the fungal toxin α-amanitin, the tunability of the active site by the elongation factor TFIIS, the recognition of DNA lesions and the use of RNA as a template.

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Language(s): eng - English
 Dates: 2009-02
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1107/S0907444908039875
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Title: Acta Crystallographica Section D: Biological Crystallography
Source Genre: Journal
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Pages: - Volume / Issue: 65 (2) Sequence Number: - Start / End Page: 112 - 120 Identifier: -