Propionylation

from Wikipedia, the free encyclopedia

The propionylation is a post-translational modification of proteins .

properties

Propionylation occurs in prokaryotes and eukaryotes . In addition to acetylation , butyrylation , crotonylation , myristylation and palmitoylation , it is a form of acylation of proteins. Propionylation takes place both at the ε- amino group of lysines and at the N terminus . Propionylated proteins in eukaryotes are, for example, histones . Propionylation in eukaryotes is presumably catalyzed by the enzymes p300 and CREB binding protein using propionyl-CoA . At the N terminus, the propionylation is catalyzed by Naa10p (synonym NatA, from N-terminal acetyltransferase A ). Compared to N -terminal acetylation, N -terminal propionylation of proteins occurs rarely, corresponding to the 20-fold higher concentration of acetyl-CoA compared to propionyl-CoA in the cell.

Individual evidence

  1. ↑ a b 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).
  2. ↑ a b c d Y. Chen, R. Sprung, Y. Tang, H. Ball, B. Sangras, SC Kim, JR Falck, J. Peng, W. Gu, Y. Zhao: Lysine propionylation and butyrylation are novel post -translational modifications in histones. In: Molecular & cellular proteomics: MCP. Volume 6, number 5, May 2007, pp. 812-819, doi : 10.1074 / mcp.M700021-MCP200 , PMID 17267393 , PMC 2911958 (free full text).
  3. ^ BR Sabari, D. Zhang, CD Allis, Y. Zhao: Metabolic regulation of gene expression through histone acylations. In: Nature reviews. Molecular cell biology. Volume 18, number 2, 02 2017, pp. 90-101, doi : 10.1038 / nrm.2016.140 , PMID 27924077 , PMC 5320945 (free full text).
  4. ↑ a b J. G. Tooley, CE Schaner Tooley: New roles for old modifications: emerging roles of N-terminal post-translational modifications in development and disease. In: Protein science: a publication of the Protein Society. Volume 23, number 12, December 2014, pp. 1641–1649, doi : 10.1002 / pro.2547 , PMID 25209108 , PMC 4253806 (free full text).
  5. ^ S. Zhao, X. Zhang, H. Li: Beyond histone acetylation-writing and erasing histone acylations. In: Current opinion in structural biology. Volume 53, 12 2018, pp. 169–177, doi : 10.1016 / j.sbi.2018.10.001 , PMID 30391813 .
  6. ^ S. Liu, W. Chang, Y. Jin, C. Feng, S. Wu, J. He, T. Xu: The function of histone acetylation in cervical cancer development. In: Bioscience Reports . Volume 39, number 4, April 2019, p., Doi : 10.1042 / BSR20190527 , PMID 30886064 , PMC 6465204 (free full text).
  7. ^ S. Lee: Post-translational modification of proteins in toxicological research: focus on lysine acylation. In: Toxicological research. Volume 29, number 2, June 2013, pp. 81–86, doi : 10.5487 / TR.2013.29.2.081 , PMID 24278632 , PMC 3834447 (free full text).
  8. ^ H. Foyn, P. Van Damme, SI Støve, N. Glomnes, R. Evjenth, K. Gevaert, T. Arnesen: Protein N-terminal acetyltransferases act as N-terminal propionyltransferases in vitro and in vivo. In: Molecular & cellular proteomics: MCP. Volume 12, number 1, January 2013, pp. 42-54, doi : 10.1074 / mcp.M112.019299 , PMID 23043182 , PMC 3536908 (free full text).