2ja6: Difference between revisions

Revision as of 19:01, 21 February 2008

CPD LESION CONTAINING RNA POLYMERASE II ELONGATION COMPLEX B

OverviewOverview

Cells use transcription-coupled repair (TCR) to efficiently eliminate DNA lesions such as ultraviolet light-induced cyclobutane pyrimidine dimers (CPDs). Here we present the structure-based mechanism for the first step in eukaryotic TCR, CPD-induced stalling of RNA polymerase (Pol) II. A CPD in the transcribed strand slowly passes a translocation barrier and enters the polymerase active site. The CPD 5'-thymine then directs uridine misincorporation into messenger RNA, which blocks translocation. Artificial replacement of the uridine by adenosine enables CPD bypass; thus, Pol II stalling requires CPD-directed misincorporation. In the stalled complex, the lesion is inaccessible, and the polymerase conformation is unchanged. This is consistent with nonallosteric recruitment of repair factors and excision of a lesion-containing DNA fragment in the presence of Pol II.

About this StructureAbout this Structure

2JA6 is a Protein complex structure of sequences from Saccharomyces cerevisiae with and as ligands. Active as DNA-directed RNA polymerase, with EC number 2.7.7.6 Known structural/functional Site: . Full crystallographic information is available from OCA.

ReferenceReference

CPD damage recognition by transcribing RNA polymerase II., Brueckner F, Hennecke U, Carell T, Cramer P, Science. 2007 Feb 9;315(5813):859-62. PMID:17290000

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 ==Overview==
-Cells use transcription-coupled repair (TCR) to efficiently eliminate DNA, lesions such as ultraviolet light-induced cyclobutane pyrimidine dimers, (CPDs). Here we present the structure-based mechanism for the first step, in eukaryotic TCR, CPD-induced stalling of RNA polymerase (Pol) II. A CPD, in the transcribed strand slowly passes a translocation barrier and enters, the polymerase active site. The CPD 5'-thymine then directs uridine, misincorporation into messenger RNA, which blocks translocation., Artificial replacement of the uridine by adenosine enables CPD bypass;, thus, Pol II stalling requires CPD-directed misincorporation. In the, stalled complex, the lesion is inaccessible, and the polymerase, conformation is unchanged. This is consistent with nonallosteric, recruitment of repair factors and excision of a lesion-containing DNA, fragment in the presence of Pol II.
+Cells use transcription-coupled repair (TCR) to efficiently eliminate DNA lesions such as ultraviolet light-induced cyclobutane pyrimidine dimers (CPDs). Here we present the structure-based mechanism for the first step in eukaryotic TCR, CPD-induced stalling of RNA polymerase (Pol) II. A CPD in the transcribed strand slowly passes a translocation barrier and enters the polymerase active site. The CPD 5'-thymine then directs uridine misincorporation into messenger RNA, which blocks translocation. Artificial replacement of the uridine by adenosine enables CPD bypass; thus, Pol II stalling requires CPD-directed misincorporation. In the stalled complex, the lesion is inaccessible, and the polymerase conformation is unchanged. This is consistent with nonallosteric recruitment of repair factors and excision of a lesion-containing DNA fragment in the presence of Pol II.
 ==About this Structure==
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 [[Category: zinc-finger]]
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