Synthesis of Two Polypeptide Subunits of an Aminoacyl tRNA Synthetase as a Single Polypeptide Chain
- 1 October 1983
- journal article
- research article
- Published by Taylor & Francis in Journal of Biomolecular Structure and Dynamics
- Vol. 1 (1) , 225-229
- https://doi.org/10.1080/07391102.1983.10507436
Abstract
E. coli aminoacyl tRNA synthetases are typically comprised of a single type of polypeptide chain. Glycine tRNA synthetase is an exception, and is comprised of two different subunits. Previous work showed that glyS encodes both subunits in a tandem arrangement of coding regions which are in the same reading frame. Nine nucleotides separate the TAA stop of the first coding segment (α-subunit) from the ATG start of the second one (β-subunit). A plasmid containing glyS was put into four different ochre suppressor strains. In three of them, significant quantities of an α-beta; fusion protein were synthesized in maxicells, in genetic backgrounds which retained cellular proteases. This shows that the fusion protein is stable in vivo and suggests that Gly-tRNA synthetase is operationally a single polypeptide which is the ancestor of the two subunits.This publication has 17 references indexed in Scilit:
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