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Published on: January 31, 2018
Post-translational modifications of lysine in DNA-damage repair
Snehajyoti Chatterjee1, Parijat Senapati, Tapas K Kundu
1Transcription and Disease Laboratory, Molecular Biology and Genetics Unit, Jawaharlal Nehru Centre for Advanced Scientific Research, Jakkur (P.O.), Bangalore 560 064, Karnataka, India.
Abstract:
DNA damage in cells is often the result of constant genotoxic insult. Nevertheless, efficient DNA repair pathways are able to maintain genomic integrity. Over the past decade it has been revealed that it is not only kinase signalling pathways which play a central role in this process, but also the different post-translational modifications at lysine residues of histone (chromatin) and non-histone proteins. These lysine modifications include acetylation, methylation, ubiquitination and SUMOylation. Genomic instability is often the major cause of different diseases, especially cancer, where lysine modifications are altered and thereby have an impact on the various DNA repair mechanisms. This chapter will discuss the recent advances in our understanding of the role of different lysine modifications in DNA repair and its physiological consequences.
Insights
Cellular DNA repair pathways maintain genomic integrity through post-translational modifications at lysine residues. These lysine modifications are crucial for DNA repair and impact diseases like cancer.
Area of Science:
- Molecular Biology
- Biochemistry
- Genetics
Background:
- Cells face constant genotoxic insults, necessitating efficient DNA repair mechanisms.
- Kinase signaling pathways are known regulators of DNA repair.
- Emerging evidence highlights the role of post-translational modifications (PTMs) on lysine residues in DNA repair.
Purpose of the Study:
- To review recent advances in understanding the role of lysine modifications in DNA repair.
- To discuss the physiological consequences of altered lysine modifications in genomic instability and disease, particularly cancer.
Main Methods:
- Literature review of recent studies on lysine modifications and DNA repair.
- Analysis of the impact of specific lysine modifications (acetylation, methylation, ubiquitination, SUMOylation) on DNA repair pathways.
- Examination of the link between altered lysine modifications, genomic instability, and cancer.
Main Results:
- Post-translational modifications of lysine residues on histones and non-histone proteins are critical for DNA repair.
- Specific lysine modifications, including acetylation, methylation, ubiquitination, and SUMOylation, directly influence DNA repair processes.
- Dysregulation of these lysine modifications is implicated in genomic instability and the development of cancer.
Conclusions:
- Lysine modifications are integral components of DNA repair pathways, essential for maintaining genomic stability.
- Altered lysine modifications contribute to disease pathogenesis, especially in cancer, by affecting DNA repair efficacy.
- Further research into lysine modifications offers potential therapeutic strategies for cancer and other diseases associated with genomic instability.
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