Article abstract


Nature Structural & Molecular Biology 14, 1127 - 1133 (2007)
Published online: 11 November 2007 | doi:10.1038/nsmb1314

Mechanism of transcriptional stalling at cisplatin-damaged DNA

Gerke E Damsma1,2, Aaron Alt1, Florian Brueckner1,2, Thomas Carell1 & Patrick Cramer1,2


The anticancer drug cisplatin forms 1,2-d(GpG) DNA intrastrand cross-links (cisplatin lesions) that stall RNA polymerase II (Pol II) and trigger transcription-coupled DNA repair. Here we present a structure-function analysis of Pol II stalling at a cisplatin lesion in the DNA template. Pol II stalling results from a translocation barrier that prevents delivery of the lesion to the active site. AMP misincorporation occurs at the barrier and also at an abasic site, suggesting that it arises from nontemplated synthesis according to an 'A-rule' known for DNA polymerases. Pol II can bypass a cisplatin lesion that is artificially placed beyond the translocation barrier, even in the presence of a GdotA mismatch. Thus, the barrier prevents transcriptional mutagenesis. The stalling mechanism differs from that of Pol II stalling at a photolesion, which involves delivery of the lesion to the active site and lesion-templated misincorporation that blocks transcription.

Top
  1. Center for Integrated Protein Science CIPSM, Department of Chemistry and Biochemistry, Ludwig-Maximilians-Universität München, Feodor-Lynen-Strasse 25, 81377 Munich, Germany.
  2. Gene Center Munich, Ludwig-Maximilians-Universität München, Feodor-Lynen-Strasse 25, 81377 Munich, Germany.

Correspondence to: Thomas Carell1 e-mail: thomas.carell@cup.uni-muenchen.de

Correspondence to: Patrick Cramer1,2 e-mail: cramer@LMB.uni-muenchen.de



MORE ARTICLES LIKE THIS

These links to content published by NPG are automatically generated.

NEWS AND VIEWS

Research highlights

Nature Structural & Molecular Biology News and Views (01 Mar 2007)


Extra navigation

Subscribe to Nature Structural & Molecular Biology

Subscribe

Open Innovation Challenges

ADVERTISEMENT