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Protein Modification by RNA‐Dependent Posttranslational Aminoacylation in Synaptoplasm
Author(s) -
Gower David J.,
Tytell Michael
Publication year - 1986
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1986.tb04514.x
Subject(s) - aminoacylation , puromycin , biochemistry , ribonuclease , ribosome , arginine , protein biosynthesis , transfer rna , rna , translation (biology) , acylation , amino acid , biology , chemistry , aminoacyl trna , microbiology and biotechnology , messenger rna , gene , catalysis
A soluble enzyme system that posttranslationally adds [ 3 H]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 postranslational amino acylation is used by the mammalian neuron for protein processing at the synaptic terminal.