Protein modification by RNA-dependent posttranslational aminoacylation in synaptoplasm.
A soluble enzyme system that posttranslationally adds [3H]arginine to proteins in a ribosome-free preparation of guinea pig synaptoplasm is described. The reaction in synaptoplasm is inhibited by the addition of ribonuclease-A and puromycin, indicating tRNA dependence. A limited number of proteins in synaptoplasm (molecular weights of 20, 37, and 50 kilodaltons) were found to accept arginine. We suggest that RNA-dependent posttranslational amino acylation is used by the mammalian neuron for protein processing at the synaptic terminal.
D000215:Acylation; D000818:Animals; D001120:Arginine / Q000378:metabolism*; D001921:Brain / Q000378:metabolism*; D003593:Cytoplasm / Q000378:metabolism; D006168:Guinea Pigs; D007526:Isoelectric Point; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D011499:Protein Processing, Post-Translational / Q000187:drug effects; D011691:Puromycin / Q000494:pharmacology; D012343:RNA, Transfer / Q000378:metabolism*; D012260:Ribonucleases / Q000494:pharmacology; D013574:Synaptosomes / Q000378:metabolism*
D009419:Nerve Tissue Proteins; D011691:Puromycin; D012343:RNA, Transfer; D001120:Arginine; D012260:Ribonucleases