Dynamics in uracil base excision repair intrinsic dynamics drive the search for a damaged base

Joshua I. Friedman, James T. Stivers

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Abstract

The base excision repair enzyme human uracil DNA glycosylase (hUNG) exhibits dynamic fluctuations when bound to DNA that are consistent with transitioning between linear scanning and a pausing mode in which extrahelical thymine and uracil bases are interrogated. The absence of these motions in free UNG suggests that the enzyme uses the favorable free energy of DNA binding to loosen its own structure and activate dynamic modes necessary for the identification of damaged uracil bases.

Original languageEnglish (US)
Title of host publicationStructural Biology of DNA Damage and Repair
PublisherAmerican Chemical Society
Pages47-58
Number of pages12
ISBN (Print)9780841225749
DOIs
StatePublished - Jun 1 2010

Publication series

NameACS Symposium Series
Volume1041
ISSN (Print)0097-6156
ISSN (Electronic)1947-5918

ASJC Scopus subject areas

  • Chemistry(all)
  • Chemical Engineering(all)

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  • Cite this

    Friedman, J. I., & Stivers, J. T. (2010). Dynamics in uracil base excision repair intrinsic dynamics drive the search for a damaged base. In Structural Biology of DNA Damage and Repair (pp. 47-58). (ACS Symposium Series; Vol. 1041). American Chemical Society. https://doi.org/10.1021/bk-2010-1041.ch004