Quantitative analysis of deoxynucleotide substitutions in the codon-anticodon helix.
The role of 2' hydroxyl groups in the codon-anticodon helix was evaluated by introducing single deoxynucleotides into each of the six positions in the helix and measuring the affinity of tRNA to either the A site or the P site of Escherichia coli 70S ribosomes. In perfect agreement with the X-ray structure of the Thermus thermophilus 30S subunit, A site binding was weaker in five of the six positions but P site binding was unaffected. Since the addition of paromomycin restores A site binding, it appears that the deoxynucleotide substituted complexes are impaired in their ability to promote the ribosomal conformational change that accompanies tRNA binding.
Fahlman
Richard P
RP
Department of Biochemistry, Molecular Biology, Cell Biology, Northwestern University, Evanston, IL 60208, USA.
Olejniczak
Mikołaj
M
Uhlenbeck
Olke C
OC
D000926:Anticodon; D003062:Codon; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D009711:Nucleotides / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D012343:RNA, Transfer / Q000378:metabolism; D012270:Ribosomes / Q000737:chemistry / Q000378:metabolism; D016963:Thermus thermophilus / Q000378:metabolism
D000926:Anticodon; D003062:Codon; D009711:Nucleotides; D012343:RNA, Transfer