Noncatalytic Domains in DNA Glycosylases | Sciact - CRIS-system of Boreskov Institute of Catalysis

Noncatalytic Domains in DNA Glycosylases Full article

Journal

International Journal of Molecular Sciences
ISSN: 1422-0067 , E-ISSN: 1661-6596

Output data

Year: 2022, Volume: 23, Number: 13, Article number : 7286, Pages count : 22 DOI: 10.3390/ijms23137286

Tags

DNA repair; base excision repair; DNA glycosylases; noncatalytic protein domains; intrinsically disordered protein regions; protein–protein interactions; post-translational modifications; DNA binding; lesion search in DNA

Authors

Torgasheva Natalia A. ¹ , Diatlova Evgeniia A. ^2,1 , Grin Inga R. ¹ , Endutkin Anton V. ¹ , Mechetin Grigory V. ¹ , Vokhtantsev Ivan P. ^2,1 , Yudkina Anna V. ¹ , Zharkov Dmitry O. ^2,1

Affiliations

1	SB RAS Institute of Chemical Biology and Fundamental Medicine, 8 Lavrentieva Avenue, 630090 Novosibirsk, Russia
2	Department of Natural Sciences, Novosibirsk State University, 2 Pirogova Street, 630090 Novosibirsk, Russia

Many proteins consist of two or more structural domains: separate parts that have a defined structure and function. For example, in enzymes, the catalytic activity is often localized in a core fragment, while other domains or disordered parts of the same protein participate in a number of regulatory processes. This situation is often observed in many DNA glycosylases, the proteins that remove damaged nucleobases thus initiating base excision DNA repair. This review covers the present knowledge about the functions and evolution of such noncatalytic parts in DNA glycosylases, mostly concerned with the human enzymes but also considering some unique members of this group coming from plants and prokaryotes.

Torgasheva N.A. , Diatlova E.A. , Grin I.R. , Endutkin A.V. , Mechetin G.V. , Vokhtantsev I.P. , Yudkina A.V. , Zharkov D.O.
Noncatalytic Domains in DNA Glycosylases
International Journal of Molecular Sciences. 2022. V.23. N13. 7286 :1-22. DOI: 10.3390/ijms23137286 WOS Scopus РИНЦ AN OpenAlex

Submitted:	May 30, 2022
Accepted:	Jun 29, 2022
Published online:	Jun 30, 2022
Published print:	Jul 1, 2022

Web of science:	WOS:000825697400001
Scopus:	2-s2.0-85133136227
Elibrary:	49152086
Chemical Abstracts:	2022:1822483
OpenAlex:	W4283742826

DB	Citing
OpenAlex	3
Web of science	3
Scopus	3