title: tRNA residues that have coevolved with their anticodon to ensure uniform and accurate codon recognition.
abstract: The structure, phylogeny and in vivo function of the base pair formed between nucleotides 32 and 38 of the tRNA anticodon loop are reviewed. The A32-U38 pair, which is highly conserved in tRNA2(Ala) and sometimes observed in tRNA2(Pro), was recently found to decrease the affinity of tRNAs to the ribosomal A site relative to other 32-38 combinations. This suggests that the role of 32-38 pair is to tune the tRNA affinity in the A site to a uniform value. New experiments presented here show that the U32C mutation in tRNA1(Gly) increases its affinity to the cognate codon and to codons with third position mismatches in the A site. This suggests that one reason for uniform tRNA binding to evolve was to avoid incorrect codon recognition.
authors.affiliation: Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, IL 60208, USA.
authors.forename: Mikołaj
authors.initials: M
authors.lastname: Olejniczak
authors.forename: Olke C
authors.initials: OC
authors.lastname: Uhlenbeck
mesh_terms: D000926:Anticodon / Q000235:genetics*; D020029:Base Pairing / Q000235:genetics; D003062:Codon / Q000235:genetics*; D019143:Evolution, Molecular; D010802:Phylogeny; D014176:Protein Biosynthesis / Q000235:genetics; D012343:RNA, Transfer / Q000235:genetics* / Q000378:metabolism; D012270:Ribosomes / Q000235:genetics / Q000378:metabolism
chemical_list: D000926:Anticodon; D003062:Codon; D012343:RNA, Transfer