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| [[Image:2ja6.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2ja6| PDB=2ja6 | SCENE= }} | | {{STRUCTURE_2ja6| PDB=2ja6 | SCENE= }} |
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| '''CPD LESION CONTAINING RNA POLYMERASE II ELONGATION COMPLEX B'''
| | ===CPD LESION CONTAINING RNA POLYMERASE II ELONGATION COMPLEX B=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17290000}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17290000 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17290000}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Zinc]] | | [[Category: Zinc]] |
| [[Category: Zinc-finger]] | | [[Category: Zinc-finger]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:35:10 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:41:42 2008'' |