Succinylation
Succinylation is a posttranslational modification where a succinyl group (-CO-CH2-CH2-CO-) 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 and introduces a relatively large structural moiety (bigger than during acetylation or methylation), 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
- ↑ 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. 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.
External links
|
|---|
| | General | |
|---|
| | N terminus | |
|---|
| | C terminus | |
|---|
| | Single specific AAs | |
|---|
| | Crosslinks between two AAs | | |
|---|
| | |
|---|
| |
- Lysine tyrosylquinone (LTQ) formation
|
|---|
| | |
|---|
|
|---|
| Three consecutive AAs
(chromophore formation) | |
|---|
| | Crosslinks between four AAs | |
|---|
|