Nucleic Acids Research, Vol 25, Issue 4 787-793, Copyright © 1997 by Oxford University Press
CP Selby, R Drapkin, D Reinberg and A Sancar
Bulky lesions in the template strand block the progression of RNA
polymerase II (RNAP II) and are repaired more rapidly than lesions in the
non-transcribed strand, which do not block transcription. In order to
better understand the basis of this transcription-coupled repair we
developed an in vitro system with purified transcription and nucleotide
excision repair proteins and a plasmid containing the adenovirus major late
promoter and a thymine dimer in the template strand downstream of the
transcription start site. The footprint of RNAP II stalled at the thymine
dimer, obtained using DNase I, lambda exonuclease and T4 polymerase
3'-->5'exonuclease, covers approximately 40 nt and is nearly symmetrical
around the dimer. The ternary complex formed at the lesion site is rather
stable, with a half-life of approximately 20 h. Surprisingly, addition of
human repair proteins results in repair of transcription-blocking dimers in
the ternary complex. The blocked polymerase neither inhibits nor stimulates
repair and repair is observed in the absence of CSB protein, the putative
human transcription-repair coupling factor.
ARTICLES
RNA polymerase II stalled at a thymine dimer: footprint and effect on excision repair
Department of Biochemistry and Biophysics, University of North Carolina School of Medicine, Chapel Hill 27599, USA.
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