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Misaminoacylation and transamidation are required for protein biosynthesis in Lactobacillus bulgaricus
1Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.
Biochimie
|March 1, 1988
Abstract:
Aminoacylation studies with Lactobacillus bulgaricus show that this organism possesses glutamyl-tRNA synthetase activity; however, glutamyl-tRNA synthetase activity cannot be demonstrated. Instead, Glu-tRNAGln, which is formed by glutamyl-tRNA synthetase, is amidated by a specific amidotransferase to Gln-tRNAGln. The amide donor in this reaction is glutamine. Thus, Gln-tRNAGln in this organism is not formed by direct glutaminylation of tRNAGln, but instead by a pathway which involves misaminoacylation and transamidation.