Author:
Xu Hong,Chen Xuanyi,Xu Xiaoli,Shi Rongyi,Suo Shasha,Cheng Kaiying,Zheng Zhiguo,Wang Meixia,Wang Liangyan,Zhao Ye,Tian Bing,Hua Yuejin
Abstract
Abstract
Lysine acetylation and succinylation are major types of protein acylation that are important in many cellular processes including gene transcription, cellular metabolism, DNA damage response. Malfunctions in these post-translational modifications are associated with genome instability and disease in higher organisms. In this study, we used high-resolution nano liquid chromatography-tandem mass spectrometry combined with affinity purification to quantify the dynamic changes of protein acetylation and succinylation in response to ultraviolet (UV)-induced cell stress. A total of 3345 acetylation sites in 1440 proteins and 567 succinylation sites in 246 proteins were identified, many of which have not been reported previously. Bioinformatics analysis revealed that these proteins are involved in many important biological processes, including cell signalling transduction, protein localization and cell metabolism. Crosstalk analysis between these two modifications indicated that modification switches might regulate protein function in response to UV-induced DNA damage. We further illustrated that FEN1 acetylation at different sites could lead to different cellular phenotypes, suggesting the multiple function involvement of FEN1 acetylation under DNA damage stress. These systematic analyses provided valuable resources and new insight into the potential role of lysine acetylation and succinylation under physiological and pathological conditions.
Publisher
Springer Science and Business Media LLC
Reference30 articles.
1. Lodish, H. et al. Molecular Biology of the Cell, p963. WH Freeman: New York, NY. 5th ed. (2004).
2. Acharya, P. V. The isolation and partial characterization of age-correlated oligo-deoxyribo-ribonucleotides with covalently linked aspartyl-glutamyl polypeptides. Johns Hopkins medical journal. (1), 254–260 (1972).
3. O’Brien, P. J. Catalytic promiscuity and the divergent evolution of DNA repair enzymes. Chem Rev. 106(2), 720–752 (2006).
4. Böhm, S. & Bernstein, K. A. The role of post-translational modifications in fine-tuning BLM helicase function during DNA repair. DNA repair. 22, 123–132 (2014).
5. Gianazza, E. Crawford, J. & Miller, I. Detecting oxidative post-translational modifications in proteins. Amino Acids. 33, 51–56 (2007).
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