In biochemistry, succinylation is a posttranslational modification where a succinyl group (−CO−CH2−CH2−CO2H) is added to a lysine residue of a protein molecule. This modification is found in many proteins, including histones.1 The potential role of succinylation is under investigation, but as addition of succinyl group changes lysine's charge from +1 to −1 (at physiological pH) and introduces a relatively large structural moiety (100 Da), bigger than acetylation (42 Da) or methylation (14 Da), it is expected to lead to more significant changes in protein structure and function.2
By analogy to acetylation, it has been suggested that succinyl-CoA is the cofactor of enzyme-mediated lysine succinylation.
References
References
- Xie, Z.; Dai, J.; Dai, L.; Tan, M.; Cheng, Z.; Wu, Y.; Boeke, J. D.; Zhao, Y. (2012). "Lysine succinylation and lysine malonylation in histones". Molecular & Cellular Proteomics. 11 (5): 100–7. doi:10.1074/mcp.M111.015875. PMC 3418837. PMID 22389435.
- Zhang, Z.; Tan, M.; Xie, Z.; Dai, L.; Chen, Y.; Zhao, Y. (2010). "Identification of lysine succinylation as a new post-translational modification". Nature Chemical Biology. 7 (1): 58–63. doi:10.1038/nchembio.495. PMC 3065206. PMID 21151122.