Structure, function and evolution of the Helix-hairpin-Helix DNA glycosylase superfamily: Piecing together the evolutionary puzzle of DNA base damage repair mechanisms.

Autor: Trasviña-Arenas CH; Department of Chemistry, University of California, Davis, CA 95616, U.S.A.. Electronic address: trasvina@ucdavis.edu., Demir M; Department of Chemistry, University of California, Davis, CA 95616, U.S.A., Lin WJ; Department of Chemistry, University of California, Davis, CA 95616, U.S.A., David SS; Department of Chemistry, University of California, Davis, CA 95616, U.S.A.. Electronic address: ssdavid@ucdavis.edu.
Jazyk: angličtina
Zdroj: DNA repair [DNA Repair (Amst)] 2021 Dec; Vol. 108, pp. 103231. Date of Electronic Publication: 2021 Sep 25.
DOI: 10.1016/j.dnarep.2021.103231
Abstrakt: The Base Excision Repair (BER) pathway is a highly conserved DNA repair system targeting chemical base modifications that arise from oxidation, deamination and alkylation reactions. BER features lesion-specific DNA glycosylases (DGs) which recognize and excise modified or inappropriate DNA bases to produce apurinic/apyrimidinic (AP) sites and coordinate AP-site hand-off to subsequent BER pathway enzymes. The DG superfamilies identified have evolved independently to cope with a wide variety of nucleobase chemical modifications. Most DG superfamilies recognize a distinct set of structurally related lesions. In contrast, the Helix-hairpin-Helix (HhH) DG superfamily has the remarkable ability to act upon structurally diverse sets of base modifications. The versatility in substrate recognition of the HhH-DG superfamily has been shaped by motif and domain acquisitions during evolution. In this paper, we review the structural features and catalytic mechanisms of the HhH-DG superfamily and draw a hypothetical reconstruction of the evolutionary path where these DGs developed diverse and unique enzymatic features.
(Copyright © 2021 The Authors. Published by Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
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