PMID:9371759
| Citation |
Schnitzer, W and von Ahsen, U (1997) Identification of specific Rp-phosphate oxygens in the tRNA anticodon loop required for ribosomal P-site binding. Proc. Natl. Acad. Sci. U.S.A. 94:12823-8 |
|---|---|
| Abstract |
tRNA binding to the ribosomal P site is dependent not only on correct codon-anticodon interaction but also involves identification of structural elements of tRNA by the ribosome. By using a phosphorothioate substitution-interference approach, we identified specific nonbridging Rp-phosphate oxygens in the anticodon loop of tRNA(Phe) from Escherichia coli which are required for P-site binding. Stereospecific involvement of phosphate oxygens at these positions was confirmed by using synthetic anticodon arm analogues at which single Rp- or Sp-phosphorothioates were incorporated. Identical interference results with yeast tRNA(Phe) and E. coli tRNA(fMet) indicate a common backbone conformation or common recognition elements in the anticodon loop of tRNAs. N-ethyl-N-nitrosourea modification-interference experiments with natural tRNAs point to the importance of the same phosphates in the loop. Guided by the crystal structure of tRNA(Phe), we propose that specific Rp-phosphate oxygens are required for anticodon loop ("U-turn") stabilization or are involved in interactions with the ribosome on correct tRNA-mRNA complex formation. |
| Links | |
| Keywords |
Anticodon; Binding Sites; Escherichia coli/genetics; Ethylnitrosourea/chemistry; Oxygen/metabolism; RNA, Transfer, Met/chemistry; RNA, Transfer, Met/genetics; RNA, Transfer, Phe/chemistry; RNA, Transfer, Phe/genetics; Ribosomal Proteins/metabolism; Ribosomes/metabolism; Saccharomyces cerevisiae/genetics; Thionucleotides/metabolism |
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