Protein Modification by RNA-Dependent Posttranslational Aminoacylation in Synaptoplasm |
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| Authors: | David J Gower† Michael Tytell† |
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| Institution: | Section on Neurosurgery, Department of Surgery, Bowman Gray School of Medicine, Winston-Salem, North Carolina, U.S.A.;Department of Anatomy, Wake Forest University Medical Center, Bowman Gray School of Medicine, Winston-Salem, North Carolina, U.S.A. |
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| Abstract: | 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. |
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| Keywords: | Aminoacylation tRNA Synaptosome Guinea pig Posttranslational protein modification |
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