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Single Qdot-labeled glycosylase molecules use a wedge amino acid to probe for lesions while scanning along DNA.

Dunn, Andrew R and Kad, Neil M and Nelson, Shane R and Warshaw, David M and Wallace, Susan S (2011) 'Single Qdot-labeled glycosylase molecules use a wedge amino acid to probe for lesions while scanning along DNA.' Nucleic acids research, 39 (17). pp. 7487-7498. ISSN 1362-4962

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Abstract

Within the base excision repair (BER) pathway, the DNA N-glycosylases are responsible for locating and removing the majority of oxidative base damages. Endonuclease III (Nth), formamidopyrimidine DNA glycosylase (Fpg) and endonuclease VIII (Nei) are members of two glycosylase families: the helix-hairpin-helix (HhH) superfamily and the Fpg/Nei family. The search mechanisms employed by these two families of glycosylases were examined using a single molecule assay to image quantum dot (Qdot)-labeled glycosylases interacting with YOYO-1 stained λ-DNA molecules suspended between 5 µm silica beads. The HhH and Fpg/Nei families were found to have a similar diffusive search mechanism described as a continuum of motion, in keeping with rotational diffusion along the DNA molecule ranging from slow, sub-diffusive to faster, unrestricted diffusion. The search mechanism for an Fpg variant, F111A, lacking a phenylalanine wedge residue no longer displayed slow, sub-diffusive motion compared to wild type, suggesting that Fpg base interrogation may be accomplished by Phe(111) insertion.

Item Type: Article
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Faculty of Science and Health > Biological Sciences, School of
Depositing User: Admin
Date Deposited: 06 Sep 2011 14:14
Last Modified: 16 Dec 2014 11:17
URI: http://repository.essex.ac.uk/id/eprint/62

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