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2ja5
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Cells use transcription-coupled repair (TCR) to efficiently eliminate DNA | + | 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== | ==About this Structure== | ||
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[[Category: zinc-finger]] | [[Category: zinc-finger]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:00:55 2008'' |
Revision as of 16:00, 21 February 2008
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CPD LESION CONTAINING RNA POLYMERASE II ELONGATION COMPLEX A
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.
About this Structure
2JA5 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.
Reference
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
Page seeded by OCA on Thu Feb 21 18:00:55 2008
Categories: DNA-directed RNA polymerase | Protein complex | Saccharomyces cerevisiae | Brueckner, F. | Carell, T. | Cramer, P. | Hennecke, U. | MG | ZN | Arrest | Cpd | Cyclobutane pyrimidine dimer | Damage recognition | Dna damage | Dna lesion | Dna-binding | Dna-directed rna polymerase | Elongation complex | Lesion recognition | Metal-binding | Misincorporation | Nuclear protein | Nucleotidyltransferase | Phosphorylation | Photolesion | Rna polymerase ii | Stalling | Tcr | Thymine dimer | Transcription | Transcription bubble | Transcription- coupled repair | Transferase | Transferase/dna/rna | Zinc | Zinc-finger
