2JA5

CPD lesion containing RNA Polymerase II elongation complex A

Summary for 2JA5

• Entry DOI: 10.2210/pdb2ja5/pdb
• Related: 1A1D 1DZF 1I3Q 1I50 1I6H 1K83 1NIK 1NT9 1PQV 1R5U 1R9S 1R9T 1SFO 1TWA 1TWC 1TWF 1TWG 1TWH 1WCM 1Y14 1Y1V 1Y1W 1Y1Y 1Y77 2B63 2B8K 2JA6 2JA7 2JA8
• Descriptor: DNA-directed RNA polymerase II subunit RPB1, DNA-directed RNA polymerases I, II, and III subunit RPABC5, DNA-directed RNA polymerase II subunit RPB11, ... (16 entities in total)
• Functional Keywords: dna-directed rna polymerase, lesion recognition, transferase/dna/rna, dna damage, zinc-finger, dna-binding, photolesion, phosphorylation, misincorporation, rna polymerase ii, transcription- coupled repair, cyclobutane pyrimidine dimer, tcr, cpd, zinc, arrest, stalling, dna lesion, metal-binding, nuclear protein, transcription bubble, nucleotidyltransferase, damage recognition, elongation complex, transferase, thymine dimer, transcription
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Nucleus: P04050 P38902 P08518 P16370 P20433 P20434 P34087 P20436; Nucleus, nucleolus : P22139 P40422 P27999; Cytoplasm : P20435
• Total number of polymer chains: 14
• Total formula weight: 526145.98

Authors

Brueckner, F.,Hennecke, U.,Carell, T.,Cramer, P. (deposition date: 2006-11-23, release date: 2007-02-20, Last modification date: 2024-10-09)

Primary citation

Brueckner, F.,Hennecke, U.,Carell, T.,Cramer, P.
Cpd Damage Recognition by Transcribing RNA Polymerase II
Science, 315:859-, 2007

PubMed Abstract: 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.

PubMed: 17290000
DOI: 10.1126/SCIENCE.1135400

Experimental method

X-RAY DIFFRACTION (3.8 Å)