4.7 Review

Noncatalytic Domains in DNA Glycosylases

期刊

出版社

MDPI
DOI: 10.3390/ijms23137286

关键词

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

资金

  1. Russian Science Foundation [21-64-00017]
  2. Russian Ministry of Science and Education [121031300056-8]

向作者/读者索取更多资源

This review provides current knowledge on the functions and evolution of noncatalytic parts in DNA glycosylases, focusing primarily on human enzymes but also considering unique members from plants and prokaryotes.
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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