Urmylation

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The Urmylierung (of English ubiquitin-related modifier , ubiquitin-like modifier ') refers to a post-translational modification of proteins , which - similar to the ubiquitination and sumoylation in some - eukaryotes are marked (yeasts and animals) for other cellular processes.

properties

During Urmylation, the protein to be degraded is coupled with the Urm1 protein by the E1-Urm ligase Uba4 . The Urm1 -modified proteins are e.g. B. Ahp1 , Mocs3 , Atpbd3 or Ctu2 . In contrast to ubiquitin, Urm1 is coupled to the C -terminal amino acid glycine via its thiocarboxylic acid .

Urm1 is involved in budding and oxidative stress in yeast .

Individual evidence

  1. ↑ AM Burroughs, LM Iyer, L. Aravind: Structure and evolution of ubiquitin and ubiquitin-related domains. In: Methods in molecular biology (Clifton, NJ). Volume 832, 2012, pp. 15-63, doi : 10.1007 / 978-1-61779-474-2_2 . PMID 22350875 .
  2. ↑ K. Furukawa, N. Mizushima, T. Noda, Y. Ohsumi: A protein conjugation system in yeast with homology to biosynthetic enzyme reaction of prokaryotes. In: The Journal of biological chemistry. Volume 275, Number 11, March 2000, pp. 7462-7465, PMID 10713047 .
  3. ↑ a b c A. G. Van der Veen, K. Schorpp, C. Schlieker, L. Buti, JR Damon, E. Spooner, HL Ploegh, S. Jentsch: Role of the ubiquitin-like protein Urm1 as a noncanonical lysine-directed protein modifier. In: Proceedings of the National Academy of Sciences . Volume 108, Number 5, February 2011, pp. 1763-1770, doi : 10.1073 / pnas.1014402108 . PMID 21209336 . PMC 3033243 (free full text).
  4. ↑ AS Goehring, DM Rivers, GF Sprague: Urmylation: a ubiquitin-like pathway that functions during invasive growth and budding in yeast. In: Molecular biology of the cell. Volume 14, Number 11, November 2003, pp. 4329-4341, doi : 10.1091 / mbc.E03-02-0079 . PMID 14551258 . PMC 266754 (free full text).
  5. ↑ F. Wang, M. Liu, R. Qiu, C. Ji: The dual role of ubiquitin-like protein Urm1 as a protein modifier and sulfur carrier. In: Protein & cell. Volume 2, number 8, August 2011, pp. 612-619, doi : 10.1007 / s13238-011-1074-6 . PMID 21904977 .