Noncatalytic Domains in DNA Glycosylases |
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| Authors: | Natalia A. Torgasheva Evgeniia A. Diatlova Inga R. Grin Anton V. Endutkin Grigory V. Mechetin Ivan P. Vokhtantsev Anna V. Yudkina Dmitry O. Zharkov |
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| Affiliation: | 1.SB RAS Institute of Chemical Biology and Fundamental Medicine, 8 Lavrentieva Avenue, 630090 Novosibirsk, Russia; (N.A.T.); (E.A.D.); (I.R.G.); (A.V.E.); (G.V.M.); (I.P.V.); (A.V.Y.);2.Department of Natural Sciences, Novosibirsk State University, 2 Pirogova Street, 630090 Novosibirsk, Russia |
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| Abstract: | 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. |
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| Keywords: | 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 |
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