2ja5

From Proteopedia

Revision as of 16:23, 5 November 2007

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 MG and ZN as ligands. Active as DNA-directed RNA polymerase, with EC number 2.7.7.6 Structure known Active Site: AC1. 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

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