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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, Kad, Neil M, Nelson, Shane R, Warshaw, David M, 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 0305-1048. E-ISSN 1362-4962. (doi:10.1093/nar/gkr459) (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)

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. (Contact us about this Publication)
Official URL
http://dx.doi.org/10.1093/nar/gkr459

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 ?-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
DOI/Identification number: 10.1093/nar/gkr459
Subjects: Q Science
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: N. Kad
Date Deposited: 15 Sep 2014 19:24 UTC
Last Modified: 29 May 2019 13:05 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/42945 (The current URI for this page, for reference purposes)
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