Identification of targets and interaction partners of arginyl-tRNA protein transferase in the moss Physcomitrella patens
Hoernstein SN, Mueller SJ, Fiedler K, Schuelke M, Vanselow JT, Schuessele C, Lang D, Nitschke R, Igloi GL, Schlosser A, Reski R.
Mol Cell Proteomics online article
Posttranslational arginylation comprises the ribosome independent incorporation of arginine residues to N-terminal amino acids mediated by arginyl-tRNA protein transferase (ATE). It represents a key position in the eukaryotic N-end rule pathway which is involved hormone signaling in plants. ATE knock out is lethal in mice and causes severe developmental defects in moss. We employed an antibody-affinity purification approach to identify targets of arginylation and interacting partners of ATE from moss and identified five targets and one interacting partner of ATE by mass spectrometry.
