Propionylation

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Protein propionylation is a post-translational modification that is characterized by the addition of a propionyl-group to a lysine amino acid residue of a protein. Lysine propionylation was first identified on histone proteins.[1] but was later also identified on non-histone proteins.[2] Although the role of protein propionylation is till not completely elucidated, histone propionylation has been observed to be a mark of active chromatin.[3] The substrate for protein propionylation is propionyl-CoA. Propionyl-CoA in the cell is metabolised by the enzyme propionyl-CoA carboxylase. In patients with propionic acidemia, a rare autosomal recessive metabolic disorder, propionyl-CoA levels elevated and increased propionylation has been observed,[4] which might contribute to the pathology in these patients.[5]

References[]

  1. ^ Chen, Y; Sprung, R; Tang, Y; Ball, H; Sangras, B; Kim, SC; Falck, JR; Peng, J; Gu, W; Zhao, Y (May 2007). "Lysine propionylation and butyrylation are novel post-translational modifications in histones". Molecular & Cellular Proteomics. 6 (5): 812–9. doi:10.1074/mcp.M700021-MCP200. PMC 2911958. PMID 17267393.
  2. ^ Cheng, Z; Tang, Y; Chen, Y; Kim, S; Liu, H; Li, SS; Gu, W; Zhao, Y (January 2009). "Molecular characterization of propionyllysines in non-histone proteins". Molecular & Cellular Proteomics. 8 (1): 45–52. doi:10.1074/mcp.M800224-MCP200. PMC 2621001. PMID 18753126.
  3. ^ Kebede, Adam F.; Nieborak, Anna; Shahidian, Lara Zorro; Le Gras, Stephanie; Richter, Florian; Gómez, Diana Aguilar; Baltissen, Marijke P.; Meszaros, Gergo; Magliarelli, Helena de Fatima; Taudt, Aaron; Margueron, Raphael (December 2017). "Histone propionylation is a mark of active chromatin". Nature Structural & Molecular Biology. 24 (12): 1048–1056. doi:10.1038/nsmb.3490. ISSN 1545-9985. PMID 29058708. S2CID 9788234.
  4. ^ Pougovkina, Olga; Te Brinke, Heleen; Wanders, Ronald J. A.; Houten, Sander M.; de Boer, Vincent C. J. (September 2014). "Aberrant protein acylation is a common observation in inborn errors of acyl-CoA metabolism". Journal of Inherited Metabolic Disease. 37 (5): 709–714. doi:10.1007/s10545-014-9684-9. ISSN 1573-2665. PMID 24531926. S2CID 26627794.
  5. ^ Lagerwaard, Bart; Pougovkina, Olga; Bekebrede, Anna F.; Brinke, Heleen; Wanders, Ronald J.A.; Nieuwenhuizen, Arie G.; Keijer, Jaap; Boer, Vincent C. J. (2020-08-17). "Increased protein propionylation contributes to mitochondrial dysfunction in liver cells and fibroblasts, but not in myotubes". Journal of Inherited Metabolic Disease: jimd.12296. doi:10.1002/jimd.12296. ISSN 0141-8955. PMID 32740932.
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