2ja6
CPD LESION CONTAINING RNA POLYMERASE II ELONGATION COMPLEX BCPD LESION CONTAINING RNA POLYMERASE II ELONGATION COMPLEX B
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCells 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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OCA- DNA-directed RNA polymerase
- Saccharomyces cerevisiae
- Brueckner, F.
- Carell, T.
- Cramer, P.
- Hennecke, U.
- 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-finger