Recognition by T factor of a tRNAphe yeast molecule recombined from 3′and 5′ halves; and its non messenger-dependent binding to ribosomes (original) (raw)

This research investigates the functionality of recombined yeast tRNAphe molecules formed from their 3׳ and 5׳ halves in relation to their specific binding to ribosomes. The findings reveal that the factor T does not differentiate between functional and nonfunctional aminoacyl-tRNAs during protein synthesis. Recombined tRNAphe can still form a ternary complex with T and GTP, allowing it to attach to ribosomes without interfering with codon-anticodon recognition, underscoring the limitations of factor T in regulating aminoacyl-tRNA entry into the ribosome.