Identification of mammalian arginyltransferases that modify a specific subset of protein substrates

作者: R. Rai , A. Kashina

DOI: 10.1073/PNAS.0504500102

关键词: TransferaseIdentification (biology)BiochemistrySaccharomyces cerevisiaeYeastCysteineArginyltransferaseBiologyProtein arginylationPeptide sequence

摘要: Posttranslational N-terminal protein arginylation, mediated by Arg-tRNA-protein transferase 1 (ATE1), is essential for cardiovascular development and angiogenesis in mammals but nonessential yeast. Evidence suggests that many proteins are arginylated vivo both yeast; however, yeast, arginylation can occur only on bearing an Asp or Glu, whereas mammals, Cys residues also targets, suggesting contributes to the role of ATE1 mammals. To date, all characterized forms yeast have been shown arginylate leaving open speculation whether possible through other components mammalian machinery Cys-specific Arg-transferase exist Here, we report identification two mice specific Cys. We show previously identified Cys-containing substrates addition Asp- Glu-containing substrates. This finding provides insights into significance possibilities determinants substrate specificity within molecule.

参考文章(16)
D K Gonda, A Bachmair, I Wünning, J W Tobias, W S Lane, A Varshavsky, Universality and structure of the N-end rule. Journal of Biological Chemistry. ,vol. 264, pp. 16700- 16712 ,(1989) , 10.1016/S0021-9258(19)84762-2
Richard L. Soffer, Peptide acceptors in the arginine transfer reaction. Journal of Biological Chemistry. ,vol. 248, pp. 2918- 2921 ,(1973) , 10.1016/S0021-9258(19)44095-7
E Balzi, M Choder, W N Chen, A Varshavsky, A Goffeau, Cloning and functional analysis of the arginyl-tRNA-protein transferase gene ATE1 of Saccharomyces cerevisiae Journal of Biological Chemistry. ,vol. 265, pp. 7464- 7471 ,(1990) , 10.1016/S0021-9258(19)39136-7
G. Bongiovanni, G. D. Fidelio, H. S. Barra, M. E. Hallak, The post-translational incorporation of arginine into a β-amyloid peptide increases the probability of α-helix formation Neuroreport. ,vol. 7, pp. 326- 328 ,(1995) , 10.1097/00001756-199512000-00078
G. Chakraborty, N.A. Ingoglia, N-terminal arginylation and ubiquitin-mediated proteolysis in nerve regeneration Brain Research Bulletin. ,vol. 30, pp. 439- 445 ,(1993) , 10.1016/0361-9230(93)90276-H
Marta E. Hallak, Guillermina Bongiovanni, Héctor S. Barra, The posttranslational arginylation of proteins in different regions of the rat brain. Journal of Neurochemistry. ,vol. 57, pp. 1735- 1739 ,(1991) , 10.1111/J.1471-4159.1991.TB06375.X
Dominik Mumberg, Rolf Muller, Martin Funk, Regulatable promoters of Saccharomyces cerevisiae: comparison of transcriptional activity and their use for heterologous expression Nucleic Acids Research. ,vol. 22, pp. 5767- 5768 ,(1994) , 10.1093/NAR/22.25.5767
Yong Tae Kwon, Anna S Kashina, Ilia V Davydov, Rong-Gui Hu, Jee Young An, Jai Wha Seo, Fangyong Du, Alexander Varshavsky, An Essential Role of N-Terminal Arginylation in Cardiovascular Development Science. ,vol. 297, pp. 96- 99 ,(2002) , 10.1126/SCIENCE.1069531
Ilia V. Davydov, Alexander Varshavsky, RGS4 Is Arginylated and Degraded by the N-end Rule Pathwayin Vitro Journal of Biological Chemistry. ,vol. 275, pp. 22931- 22941 ,(2000) , 10.1074/JBC.M001605200