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Damage detection by the UvrABC pathway: Crystal structure of UvrB bound to fluorescein‐adducted DNA
Author(s) -
Waters Timothy R.,
Eryilmaz Jitka,
Geddes Stella,
Barrett Tracey E.
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.10.051
Subject(s) - dna , dna damage , biophysics , nucleotide excision repair , fluorescein , chemistry , nucleotide , thymine , microbiology and biotechnology , biology , biochemistry , fluorescence , optics , physics , gene
UvrB is the damage recognition element of the highly conserved UvrABC pathway that functions in the removal of bulky DNA adducts. Pivotal to this is the formation of a damage detection complex that relies on the ability of UvrB to locate and sequester diverse lesions. Whilst structures of UvrB bound to DNA have recently been reported, none address the issue of lesion recognition. Here, we describe the crystal structure of UvrB bound to a pentanucleotide containing a single fluorescein‐adducted thymine that reveals a unique mechanism for damage detection entirely dependent on the exclusion of lesions larger than an undamaged nucleotide.