Noncatalytic Domains in DNA Glycosylases

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...

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Veröffentlicht in:International journal of molecular sciences 2022-06, Vol.23 (13), p.7286
Hauptverfasser: Torgasheva, Natalia A., Diatlova, Evgeniia A., Grin, Inga R., Endutkin, Anton V., Mechetin, Grigory V., Vokhtantsev, Ivan P., Yudkina, Anna V., Zharkov, Dmitry O.
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Sprache:eng
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Zusammenfassung: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.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms23137286