Sirtuins in DNA repair

Authors

  • Mateusz Kciuk Department of Molecular Biotechnology and Genetics, Faculty of Biology and Environmental Protection, University of Lodz
  • Renata Kontek Department of Molecular Biotechnology and Genetics, Faculty of Biology and Environmental Protection, University of Lodz

DOI:

https://doi.org/10.18388/pb.2020_319

Abstract

DNA repair involves number of processes required for detection and repair of DNA damage. The ability to repair existing damage is crucial
for preservation of both physical integrity of the genome and fidelity of genetic information. Genetic insults may derive from either metabolic
reactions inside the cell or come from exogenous environment. Sirtuins belong to the class of histone deacetylases that catalyze the removal
of acetyl moieties from the lysine residues of both histone and nonhistone proteins. Furthermore, some sirtuins exhibit mono-ADP-ribosyltransferase
activity that regulates activity of various proteins. The first sirtuin was identified in yeast (Saccharomyces cerevisiae), however both
prokaryotic and eukaryotic homologs of sirtuins were later discovered. Seven mammalian homologs (SIRT1-SIRT7) exist. Sirtuins represent
an emerging group of enzymes that coordinate DNA repair in respect of cellular metabolic status and may have a prominent role in neoplastic
transformation, diabetes, ageing and age-related diseases such as neurodegeneration. The aim of this paper is to review recent research on the
role of sirtuins in DNA repair processes.

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Published

2020-06-27

Issue

Vol. 66 No. 2 (2020)

Section

Articles

License

Copyright (c) 2020 Advances in Biochemistry

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