Abstract
Publisher Summary In Escherichia coli , glutamic acid and glutamine are charged respectively on tRNA Glu and tRNA Gln in reactions catalyzed by distinct enzymes. In general, each amino acid to be incorporated into proteins in E. coli or in other gram-negative bacteria is first activated by a specific aminoacyl-tRNA synthetase. The pure glutamyl-tRNA synthetase (GluRS) of Bacillus subtilis catalyzes the aminoacylation of both tRNA Glu and tRNA Gln with glutamic acid. The structural gene for the monomeric GluRS of E. coli is at the locus glt X at min 50. Using the thermosensitive mutant JP1449, altered in this locus and having a thermolabile GluRS, it is shown that the GluRS or its main product, glutamyl-tRNA, is involved in the regulation of glutamine or glutamate biosynthesis in E. coli. The structural gene of the GluRS on a 2.7 kb fragment of chromosomal DNA inserted into pBR322 is cloned in JP1449 by complementation of the ts mutation of this strain.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
