PMID:6086058

Citation	Keng, T and Schimmel, P (1983) Synthesis of two polypeptide subunits of an aminoacyl tRNA synthetase as a single polypeptide chain. J. Biomol. Struct. Dyn. 1:225-9
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 (alpha-subunit) from the ATG start of the second one (beta-subunit). A plasmid containing glyS was put into four different ochre suppressor strains. In three of them, significant quantities of an alpha-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.
Links	PubMed Online version:10.1080/07391102.1983.10507436
Keywords	Amino Acid Sequence; Amino Acyl-tRNA Synthetases/biosynthesis; Base Sequence; Escherichia coli/enzymology; Escherichia coli/genetics; Glycine-tRNA Ligase/biosynthesis; Glycine-tRNA Ligase/genetics; Molecular Sequence Data; Protein Conformation; RNA, Bacterial/genetics; RNA, Messenger/genetics; Recombinant Fusion Proteins/biosynthesis; Recombinant Fusion Proteins/genetics
edit table

Significance

You can help EcoliWiki by summarizing why this paper is useful

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Add links to pages that link here (e.g. gene, product, method pages)

See Help:References for how to manage references in EcoliWiki.