A single tRNA base pair mediates bacterial tRNA-dependent biosynthesis of asparagine

Marc Bailly (1) , Stamatina Giannouli , Mickaël Blaise (2) , Constantinos Stathopoulos , Daniel Kern (1) , Hubert Dominique Becker (1)

1 ARN - Architecture et réactivité de l'ARN
2 IRIM - Institut de Recherche en Infectiologie de Montpellier

In many prokaryotes and in organelles asparagine and glutamine are formed by a tRNA-dependent amidotransferase (AdT) that catalyzes amidation of aspartate and glutamate, respectively, mischarged on tRNA Asn and tRNA Gln. These pathways supply the deficiency of the organism in asparaginyl-and glutaminyl-tRNA synthtetases and provide the translational machinery with Asn-tRNA Asn and Gln-tRNA Gln. So far, nothing is known about the structural elements that confer to tRNA the role of a specific cofactor in the formation of the cognate amino acid. We show herein, using aspartylated tRNA Asn and tRNA Asp

Domaines: Sciences du Vivant [q-bio]

Marc Bailly, Stamatina Giannouli, Mickaël Blaise, Constantinos Stathopoulos, Daniel Kern, et al.. A single tRNA base pair mediates bacterial tRNA-dependent biosynthesis of asparagine. Nucleic Acids Research, 2006, 34 (21), pp.6083-6094. ⟨10.1093/nar/gkl622⟩. ⟨hal-02386007⟩