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

  1. ^ 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.
  2. ^ 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.

External links

Protein primary structure and posttranslational modifications
Posttranslational modification
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