The -C-C-A End of tRNA and Its Role in Protein Biosynthesis

Functional transfer RNAs with modifications in the 3'-CCA end: differential effects on aminoacylation and polypeptide synthesis.

“…1). Chemical and nuclease protection studies indicate that the 3'-CCA sequence also functions in later steps of protein synthesis: in formation of a ternary complex between aminoacyl-tRNA, elongation factor Tu, and GTP (1) and in the binding of tRNA to 23S rRNA at the A, P, and E sites of the 50S ribosomal subunit during the elongation and translocation steps of the translation cycle (2)(3)(4)(5)(6).…”

NMR reveals structural rearrangements associated to substrate insertion in nucleotide‐adding enzymes

“…1,2 This reaction is performed by the CCA-adding family of nucleotidyltransferases, which on the one hand catalyze the high-fidelity incorporation of the three nucleotides in the absence of a nucleic acid template, 3 and on the other hand act by proofreading unstable tRNAs. 4 Archeal genomes encode class I CCA-adding enzymes, 5 while class II is found in eubacteria and eukaryotes.…”

3′‐Deoxy‐3′‐aminonucleoside 5′‐triphosphates — Terminators of RNA synthesis, catalyzed by DNA‐dependent RNA polymerase from Escherichia coli

“…The modified tRNAs of this type allowed us to reveal some details of the molecular mechanism of the aminoacyl-tRNA enzymatic synthesis [ 1,2] and ribosomal synthesis of proteins [2,3]. ATP(3 'NH2) also effectively inhibited the DNAdependent RNA polymerase from the Ehrlich ascites tumour cells [4] and E. coli [5,6].…”