Participation in protein biosynthesis of transfer ribonucleic acid bearing altered 3'-terminal ribosyl residues

Separation of aminoacyl‐tRNAPhe and tRNAsPhe with partially hydrolysed 3′‐end by polyacrylamide gradient micro‐electrophoresis

“…Such modified tRNAs were used for spectroscopic [ 1,2] and biochemical investigations [3,4] as well as isomorphous substitution of tRNAphe with heavy metals for X-ray crystallographic work [5,6] . As a starting material for incorporation of CMP or AMP analogues serves a tRNA where the 3'-end is partially or completely missing.…”

Isomeric aminoacyl-tRNAs are both bound by elongation factor Tu.

“…On the basis of these observations, it was suggested (17, 18) FI. 4. Gel filtration on Sephadex G-100 of (A) tryptophanyltRNA 2b (U and (B) tryptophanyl-tRNA 3b (U) in the presence of approximately equimolar amounts of unmodified tryptophanyl-tRNA (ib) (0) and limiting amounts of EF-Tu-GTP.…”

“…Although aminoacyl-tRNA is thought to consist of a mixture of 2'-and 3'-O-aminoacyl species which equilibrate rapidly, the specificity generally associated with enzymic processes makes it not unlikely that single isomers of tRNA may be utilized exclusively for certain of the partial reactions of protein biosynthesis.' The rapid equilibration of the two isomers of aminoacyl-tRNAs has precluded a determination of positional specificities involved in such transformations, but data of this type are now accessible by the use of certain modified tRNAs, e.g., those terminating in 2'-and 3'-deoxyadenosine (1)(2)(3)(4)(5)(6). Results obtained from the study of suchmodified tRNAs have suggested, e.g., that tRNAs are aminoacylated exclusively on a single (2' or 3') OH group (7)(8)(9).…”

“…Results obtained from the study of suchmodified tRNAs have suggested, e.g., that tRNAs are aminoacylated exclusively on a single (2' or 3') OH group (7)(8)(9). The use of isomeric phenylalanyl-tRNAs has also permitted the study of positional specificities involved in the binding of (N-acetyl)phenylalanyl-tRNA to the ribosomal A-and P-sites and in participation of phenylalanyl-tRNA as an acceptor in the peptidyltransferase reaction (2,4,5).…”

Properties of Alanyl‐oligonucleotide, Puromycin, and Staphylococcus epidermidis glycyl‐tRNA in interaction with elongation factor tu:GTP complex

“…Furthermore, aminoacyl-viral RNA can form the complex [26]. Some of these observations suggest that the anticodon loop is not involved in the interaction with EF-Tu:GTP, and amino acid stem containing aminoacylated CCA is important in the complex formation [27,28].…”