Binding of complementary oligonucleotides to free and aminoacyl transfer ribonucleic acid synthetase bound transfer ribonucleic acid

Photocrosslinking analysis of the contact surface of tRNAMet in complexes with Escherichia coli methionine:tRNA ligase

“…Unlike previous studies with other tRNAs, the D arm is not involved and significant radiation damage is suffered by the tRNA which must be taken into account in the analysis. The results are consistent with and complement chemical modification studies [Schulman, L. H., & Pelka, H. (1977) Biochemistry 16, 4256], tRNAs recognized by the same enzyme (Roe et al, 1973), and (g) competitive oligonucleotide binding to indicate shielding of complementary sequences by the bound ligase (Schimmel et al, 1972). While all of these approaches are informative, they have serious limitations.…”

Aminoacyl-tRNA Synthetases: General Features and Recognition of Transfer RNAs

“…Since amino acids are attached to the 3'-termini of tRNAs, the enzymes must make contact at this point. Indeed, in some studies it has been possible to demonstrate directly that this is a contact area (220,257,284). Finally, the anticodon region is often implicated in photochemical cross-linking studies.…”

Effect of excision of the Y-base on the interaction of tRNAPhe (yeast) with phenylalanyl-tRNA synthetase (yeast).

“…We have shown previously that the Y-base is in close contact with the synthetase during complEc formation (4) and therefore can represent a point of attachment for the synthetase. The existence of a contact point in the anticodon region has been already suggested for the Ileu-specific system from E.coli (16). At present, however, it is not possible to assign the low affinity of tRNbAPhe for its cognate syntheta--y se to a definite structure of the tRNAP , since the different structural changes cannot be studied separately.…”