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Title page for ETD etd-05312018-144657

Type of Document Dissertation
Author Shi, Rongxin
URN etd-05312018-144657
Title Characterization of heat-like repeat superfamily of DNA glycosylases
Degree PhD
Department Biological Sciences
Advisory Committee
Advisor Name Title
Katherine L. Friedman Committee Chair
Benjamin Spiller Committee Member
Brandt F. Eichman Committee Member
Carmelo Rizzo Committee Member
Todd Graham Committee Member
  • DNA glycosylase
  • Base excision repair
  • AlkC
Date of Defense 2018-05-09
Availability unrestricted
DNA glycosylases preserve genome integrity and define the specificity of the base excision repair pathway for discreet, detrimental modifications. Bacterial HEAT-like repeat glycosylases AlkC and AlkD are specific for cationic alkylated nucleobases and have a distinctive HEAT-like repeat (HLR) fold. AlkD uses a unique non-base-flipping mechanism that enables excision of bulky lesions more commonly associated with nucleotide excision repair. In contrast, AlkC has a much narrower specificity for small lesions, principally N3-methyladenine. A crystal structure resembling a catalytic intermediate complex shows how AlkC uses unique HLR and immunoglobulin-like domains to induce a sharp kink in the DNA, exposing the damaged nucleobase to active site residues that project into the DNA. Genetic analysis of AlkC and AlkD in cells and comprehensive comparison of AlkC and AlkD with other, non-enzymatic HLR proteins provide the insights into protein structure/function/evolution relationships of this new superfamily of proteins.
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