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Article

UvrAB activity at a damaged DNA site: is unpaired DNA present?

The EMBO journal - 17 Feb 1997

Gordienko I, Rupp W D

Abstract excerpt

To study the activity of the Escherichia coli UvrA and UvrB nucleotide excision repair proteins during the formation of the pre-incision complex at a damaged DNA site, we used substrates with modifications around a single 2-(acetylamino)fluorene (AAF) lesion. Based on the release of AAF-containing oligonucleotides from a single-stranded DNA circle, we conclude that during interaction with our substrates UvrAB...

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Identifiers

PMID: 9049316
DOI: 10.1093/emboj/16.4.880
PMCID: PMC1169688

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UvrAB activity at a damaged DNA site: is unpaired DNA present?PMID 9049316Read ↗

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The C-terminal region of Escherichia coli UvrC contributes to the flexibility of the UvrABC nucleotide excision repair system.Semantic proximity Read ↗

Acetylaminofluorene bound to different guanines of the sequence -GGCGCC- is excised with different efficiencies by the UvrABC excision nuclease in a pattern not correlated to the potency of mutation induction.Semantic proximity Read ↗

The C-terminal zinc finger of UvrA does not bind DNA directly but regulates damage-specific DNA binding.Semantic proximity Read ↗

Helicase motifs V and VI of the Escherichia coli UvrB protein of the UvrABC endonuclease are essential for the formation of the preincision complex.Semantic proximity Read ↗

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