作者: R. Rai , A. Kashina
关键词: Transferase 、 Identification (biology) 、 Biochemistry 、 Saccharomyces cerevisiae 、 Yeast 、 Cysteine 、 Arginyltransferase 、 Biology 、 Protein arginylation 、 Peptide 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.