Arginylation
Arginylation is the process by which the amino acid arginine is attached to the N-terminal end of proteins . The attachment of this amino acid is very specific and is a post-translational modification of proteins.
The actual process of arginylation is catalyzed by the enzyme Arg transfer RNA protein transferase (Ate1). An arginyl residue is coupled to an N-terminal asparagine , glutamine or cysteine residue. This process takes place after a specific proteolysis , i.e. enzymes split the original protein, so that a peptide with these N-terminal amino acids is formed (often only the initial methionine is split off). The failure of the evolutionarily well conserved enzyme Ate1 leads to fatal malformations in the embryo in mice. Arginylation is an important modification in eukaryotes in terms of the N-end rule .
The function of the arginylation itself has not yet been clarified. Every fifth actin monomer in fibroblasts is arginylated, which has a direct effect on the increased stability of actin filaments. In the case of other proteins, arginylation seems to be more of a degradation signal for them.
literature
- ↑ P. Stöcker: Arginylation. In: Laborjournal. 10/2006, p. 40.
- ↑ M. Karakozova, M. Kozak, CC Wong, AO Bailey, JR Yates, A. Mogilner, H. Zebroski, A. Kashina: Arginylation of beta-actin regulates actin cytoskeleton and cell motility. In: Science . 313 (5784), 2006, pp. 192-196. PMID 16794040 .
- ↑ P. Bohley, J. Kopitz, G. Adam, B. Rist, F. von Appen, S. Urban: Post-translational arginylation and intracellular proteolysis. In: Biomed Biochim Acta. 50 (4-6), 1991, pp. 343-346. PMID 1801699 .
- ^ IV Davydov, A. Varshavsky : RGS4 is arginylated and degraded by the N-end rule pathway in vitro. In: J Biol Chem . 275 (30), 2000, pp. 22931-22941. PMID 10783390 .