Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
Reading and misreading 8-oxoguanine, a paradigmatic ambiguous nucleobase. / Yudkina, Anna V.; Shilkin, Evgeniy S.; Endutkin, Anton V. и др.
в: Crystals, Том 9, № 5, 269, 01.05.2019.Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
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TY - JOUR
T1 - Reading and misreading 8-oxoguanine, a paradigmatic ambiguous nucleobase
AU - Yudkina, Anna V.
AU - Shilkin, Evgeniy S.
AU - Endutkin, Anton V.
AU - Makarova, Alena V.
AU - Zharkov, Dmitry O.
N1 - Publisher Copyright: © 2019 by the authors.
PY - 2019/5/1
Y1 - 2019/5/1
N2 - 7,8-Dihydro-8-oxoguanine (oxoG) is the most abundant oxidative DNA lesion with dual coding properties. It forms both Watson–Crick (anti)oxoG:(anti)C and Hoogsteen (syn)oxoG:(anti)A base pairs without a significant distortion of a B-DNA helix. DNA polymerases bypass oxoG but the accuracy of nucleotide incorporation opposite the lesion varies depending on the polymerase-specific interactions with the templating oxoG and incoming nucleotides. High-fidelity replicative DNA polymerases read oxoG as a cognate base for A while treating oxoG:C as a mismatch. The mutagenic e_ects of oxoG in the cell are alleviated by specific systems for DNA repair and nucleotide pool sanitization, preventing mutagenesis from both direct DNA oxidation and oxodGMP incorporation. DNA translesion synthesis could provide an additional protective mechanism against oxoG mutagenesis in cells. Several human DNA polymerases of the X- and Y-families e_ciently and accurately incorporate nucleotides opposite oxoG. In this review, we address the mutagenic potential of oxoG in cells and discuss the structural basis for oxoG bypass by di_erent DNA polymerases and the mechanisms of the recognition of oxoG by DNA glycosylases and dNTP hydrolases.
AB - 7,8-Dihydro-8-oxoguanine (oxoG) is the most abundant oxidative DNA lesion with dual coding properties. It forms both Watson–Crick (anti)oxoG:(anti)C and Hoogsteen (syn)oxoG:(anti)A base pairs without a significant distortion of a B-DNA helix. DNA polymerases bypass oxoG but the accuracy of nucleotide incorporation opposite the lesion varies depending on the polymerase-specific interactions with the templating oxoG and incoming nucleotides. High-fidelity replicative DNA polymerases read oxoG as a cognate base for A while treating oxoG:C as a mismatch. The mutagenic e_ects of oxoG in the cell are alleviated by specific systems for DNA repair and nucleotide pool sanitization, preventing mutagenesis from both direct DNA oxidation and oxodGMP incorporation. DNA translesion synthesis could provide an additional protective mechanism against oxoG mutagenesis in cells. Several human DNA polymerases of the X- and Y-families e_ciently and accurately incorporate nucleotides opposite oxoG. In this review, we address the mutagenic potential of oxoG in cells and discuss the structural basis for oxoG bypass by di_erent DNA polymerases and the mechanisms of the recognition of oxoG by DNA glycosylases and dNTP hydrolases.
KW - 7,8-Dihydro-8-oxoguanine
KW - Base excision repair
KW - DNA glycosylases
KW - DNA polymerases
KW - Mutagenesis
KW - Nucleotide hydrolases
KW - Translesion DNA synthesis
KW - translesion DNA synthesis
KW - OXIDATIVELY DAMAGED DNA
KW - STEADY-STATE KINETICS
KW - ACTIVE-SITE
KW - CRYSTAL-STRUCTURE
KW - HUMAN DNA-POLYMERASE
KW - ESCHERICHIA-COLI
KW - base excision repair
KW - mutagenesis
KW - 8-Dihydro-8-oxoguanine
KW - ERROR-PRONE REPLICATION
KW - BASE EXCISION-REPAIR
KW - COLI MUTY GENE
KW - 7
KW - nucleotide hydrolases
KW - NUDIX HYDROLASE
UR - http://www.scopus.com/inward/record.url?scp=85073280411&partnerID=8YFLogxK
U2 - 10.3390/cryst9050269
DO - 10.3390/cryst9050269
M3 - Article
AN - SCOPUS:85073280411
VL - 9
JO - Crystals
JF - Crystals
SN - 2073-4352
IS - 5
M1 - 269
ER -
ID: 21856906