Reading and Misreading 8-oxoguanine, a Paradigmatic Ambiguous Nucleobase | Sciact - CRIS-system of Boreskov Institute of Catalysis

Reading and Misreading 8-oxoguanine, a Paradigmatic Ambiguous Nucleobase Review

Journal

Crystals
, E-ISSN: 2073-4352

Output data

Year: 2019, Volume: 9, Number: 5, Article number : 269, Pages count : DOI: 10.3390/cryst9050269

Tags

7,8-Dihydro-8-oxoguanine; mutagenesis; DNA polymerases; base excision repair; DNA glycosylases; nucleotide hydrolases; translesion DNA synthesis

Authors

Yudkina Anna Y. ^1,2 , Shilkin Evgeniy S. ³ , Endutkin Anton V. ^1,4 , Makarova Alena V ³ , Zharkov Dmitry O. ^1,2

Affiliations

1	Novosibirsk State University, 1 Pirogova St., 630090 Novosibirsk, Russia
2	SB RAS Institute of Chemical Biology and Fundamental Medicine, 8 Lavrentieva Ave., 630090 Novosibirsk, Russia
3	RAS Institute of Molecular Genetics, 2 Kurchatova Sq., 123182 Moscow, Russia
4	Podalirius Ltd., 77 Sacco and Vanzetti St, 630008 Novosibirsk, Russia

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 effects 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 efficiently 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 different DNA polymerases and the mechanisms of the recognition of oxoG by DNA glycosylases and dNTP hydrolases.

Yudkina A.Y. , Shilkin E.S. , Endutkin A.V. , Makarova A.V. , Zharkov D.O.
Reading and Misreading 8-oxoguanine, a Paradigmatic Ambiguous Nucleobase
Crystals. 2019. V.9. N5. 269 . DOI: 10.3390/cryst9050269 WOS Scopus OpenAlex

Submitted:	Apr 26, 2019
Accepted:	May 19, 2019
Published print:	May 23, 2019
Published online:	May 23, 2019

Web of science:	WOS:000472674400045
Scopus:	2-s2.0-85073280411
OpenAlex:	W2946277591

DB	Citing
Web of science	28
OpenAlex	33
Scopus	28