Single molecule iSCAT imaging reveals a fast, energy efficient search mode for the DNA repair protein UvrA
Author:
Affiliation:
1. School of Biological Sciences, Division of Natural Sciences, University of Kent, Canterbury CT2 7NH, UK
Abstract
Funder
University of Kent
Biotechnology and Biological Sciences Research Council
Publisher
Royal Society of Chemistry (RSC)
Subject
General Materials Science
Link
http://pubs.rsc.org/en/content/articlepdf/2022/NR/D1NR06913F
Reference43 articles.
1. Prokaryotic Nucleotide Excision Repair: The UvrABC System
2. Analyzing the Handoff of DNA from UvrA to UvrB Utilizing DNA-Protein Photoaffinity Labeling
3. The β-Hairpin Motif of UvrB Is Essential for DNA Binding, Damage Processing, and UvrC-mediated Incisions
4. Interactions between UvrA and UvrB: the role of UvrB's domain 2 in nucleotide excision repair
5. A novel repair enzyme: UVRABC excision nuclease of Escherichia coli cuts a DNA strand on both sides of the damaged region
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