Succinylation

Addition of a succinyl group to a lysine group of a protein

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

  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

  • Succinylation, Yet A Novel PTM Pathway for Biological Regulation, But Ready to Be Investigated
  • Succinyl group at ChEBI
  • The dawn of succinylation: a posttranslational modification.
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Protein primary structure and posttranslational modifications
General
  • Peptide bond
  • Protein biosynthesis
  • Proteolysis
  • Racemization
  • N–O acyl shift
N terminusC terminusSingle specific AAs
Serine/Threonine
Tyrosine
Cysteine
Aspartate
Glutamate
Asparagine
Glutamine
Lysine
Arginine
Proline
Histidine
Tryptophan
Crosslinks between two AAs
CysteineCysteine
MethionineHydroxylysine
LysineTyrosine
  • Lysine tyrosylquinone (LTQ) formation
TryptophanTryptophan
Crosslinks between three AAs
SerineTyrosineGlycine
HistidineTyrosineGlycine
  • 4-(p-hydroxybenzylidene)-5-imidazolinone (HBI) formation (chromophore)
AlanineSerineGlycine
Crosslinks between four AAs
AllysineAllysineAllysineLysine
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  • t
  • e
Chaperones/
protein folding
Heat shock proteins/
Chaperonins
Other
Protein targeting
Ubiquitin
(ubiquitylation)
Ubiquitin-like proteins
(UBL)
SUMO protein
(SUMOylation)
  • E1 SUMO-activating enzyme
  • E2 SUMO-conjugating enzyme
Other