Association of tRNA(Gln) acceptor identity with phosphate-sugar backbone interactions observed in the crystal structure of the Escherichia coli glutaminyl-tRNA synthetase-tRNA(Gln) complex.

Abstract excerpt

We isolated several mutants with nucleotide substitutions in alanine tRNA (tRNA(Ala)) that resulted in glutamine tRNA (tRNA(Gln)) acceptor identity in Escherichia coli. These substitutions were in three regions of tRNA structure not previously associated with tRNA(Gln) acceptor identity. Only the phosphate-sugar backbone moieties of these nucleotides interact with the enzyme in the previously determined X-ray...

Topics

• Amino Acyl-tRNA Synthetases
• Base Sequence
• Carbohydrate Metabolism
• Computer Simulation
• Crystallization
• Escherichia coli
• Molecular Sequence Data
• Mutation
• Nucleic Acid Conformation
• Phosphates