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Collaborative dynamic DNA scanning by nucleotide excision repair proteins investigated by single- molecule imaging of quantum-dot-labeled proteins

Kad, Neil M, Wang, Hong, Kennedy, Guy G, Warshaw, David M, Van Houten, Bennett (2010) Collaborative dynamic DNA scanning by nucleotide excision repair proteins investigated by single- molecule imaging of quantum-dot-labeled proteins. Molecular cell, 37 (5). pp. 702-713. ISSN 1097-4164. (doi:10.1016/j.molcel.2010.02.003) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:42946)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided.
Official URL:
http://dx.doi.org/10.1016/j.molcel.2010.02.003

Abstract

How DNA repair proteins sort through a genome for damage is one of the fundamental unanswered questions in this field. To address this problem, we uniquely labeled bacterial UvrA and UvrB with differently colored quantum dots and visualized how they interacted with DNA individually or together using oblique-angle fluorescence microscopy. UvrA was observed to utilize a three-dimensional search mechanism, binding transiently to the DNA for short periods (7 s). UvrA also was observed jumping from one DNA molecule to another over approximately 1 microm distances. Two UvrBs can bind to a UvrA dimer and collapse the search dimensionality of UvrA from three to one dimension by inducing a substantial number of UvrAB complexes to slide along the DNA. Three types of sliding motion were characterized: random diffusion, paused motion, and directed motion. This UvrB-induced change in mode of searching permits more rapid and efficient scanning of the genome for damage.

Item Type: Article
DOI/Identification number: 10.1016/j.molcel.2010.02.003
Subjects: Q Science
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Neil Kad
Date Deposited: 15 Sep 2014 19:26 UTC
Last Modified: 16 Nov 2021 10:17 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/42946 (The current URI for this page, for reference purposes)

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