Succinylation

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The succinylation is a post-translational modification of proteins .

properties

In succinylation, a succinyl group is coupled to a lysine in a protein via an isopeptide bond , e.g. B. in histones or glutamate dehydrogenase . The succinylation leads to a change in charge on the lysine of a protein from a positive charge on the free ε- amine to a negatively charged succinyl group. One of the two substrates in succinylation is succinyl-CoA , analogous to acetyl-CoA in acetylation , malonyl-CoA in malonylation and glutaryl-CoA in glutarylation. The biological function of succinylation is still partially unknown, mitochondrial proteins are often succinylated. In the case of oxidative stress , succinylated proteins occur more frequently. Most succinylated proteins are metabolic proteins , which suggests regulation by succinylation. Unlike the succinylation be at a succination the thiol groups of cysteines post-translationally modified with a succinyl.

Web links

Individual evidence

  1. ↑ Z. Xie, J. Dai, L. Dai, M. Tan, Z. Cheng, Y. Wu, JD Boeke, Y. Zhao: Lysine succinylation and lysine malonylation in histones. In: Molecular & cellular proteomics: MCP. Volume 11, number 5, May 2012, pp. 100-107, doi : 10.1074 / mcp.M111.015875 , PMID 22389435 , PMC 3418837 (free full text).
  2. ↑ a b c d e H. Lin, X. Su, B. He: Protein lysine acylation and cysteine ​​succination by intermediates of energy metabolism. In: ACS chemical biology. Volume 7, number 6, June 2012, pp. 947-960, doi : 10.1021 / cb3001793 , PMID 22571489 , PMC 3376250 (free full text).
  3. ↑ Z. Zhang, M. Tan, Z. Xie, L. Dai, Y. Chen, Y. Zhao: Identification of lysine succinylation as a new post-translational modification. In: Nature chemical biology. Volume 7, number 1, January 2011, pp. 58-63, doi : 10.1038 / nchembio.495 , PMID 21151122 , PMC 3065206 (free full text).
  4. ↑ KN Papanicolaou, B. O'Rourke, DB Foster: Metabolism leaves its mark on the powerhouse: recent progress in post-translational modifications of lysine in mitochondria. In: Frontiers in physiology. Volume 5, 2014, p. 301, doi : 10.3389 / fphys.2014.00301 , PMID 25228883 , PMC 4151196 (free full text).
  5. ↑ E. Mills, LA O'Neill: Succinate: a metabolic signal in inflammation. In: Trends in cell biology. Volume 24, number 5, May 2014, pp. 313-320, doi : 10.1016 / j.tcb.2013.11.008 , PMID 24361092 .