Noncatalytic Domains in DNA Glycosylases

Research output: Contribution to journalReview articlepeer-review

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.

Original languageEnglish
Article number7286
JournalInternational Journal of Molecular Sciences
Volume23
Issue number13
DOIs
Publication statusPublished - 1 Jul 2022

Keywords

  • base excision repair
  • DNA binding
  • DNA glycosylases
  • DNA repair
  • intrinsically disordered protein regions
  • lesion search in DNA
  • noncatalytic protein domains
  • post-translational modifications
  • protein–protein interactions
  • Humans
  • DNA/chemistry
  • DNA Repair
  • DNA Glycosylases/metabolism
  • DNA Damage

OECD FOS+WOS

  • 2.04 CHEMICAL ENGINEERING
  • 1.04 CHEMICAL SCIENCES
  • 1.06 BIOLOGICAL SCIENCES

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