Structure investigation of Phe-tRNAphefromE.colibound to the ribosomal A-site
Open Access
- 11 February 1983
- journal article
- research article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 11 (3) , 575-589
- https://doi.org/10.1093/nar/11.3.575
Abstract
Kethoxal modification of guanosines within phe-tRNAphe from E.Coli was studied for tRNA in the free state and specifically bound to the ribosomal A-site. Complex formation with the ribosome results in a protection from chemical modification of two distant sites in the tRNA molecule. The guanosines affected are G-18 and G-19, located in the D-loop, and G-34 in the anticodon loop. Modification of phe-tRNAphe in the absence of ribosomes leads to a destabilisation of the tRNA structure. Our data are consistent with the conclusion that mocification of G-34 at the anticodon loop triggers a conformational instability in distant parts of the tRNA molecule.Keywords
This publication has 11 references indexed in Scilit:
- Adenosine dimethylation of 16S ribosomal RNA: effect of the methylgroups on local conformational stability as deduced from electrophoretic mobility of RNA fragments in denaturing polyacrylamide gelsNucleic Acids Research, 1981
- Comparison of the structures of free and ribosome-bound tRNAPhe by using slow tritium exchange.Proceedings of the National Academy of Sciences, 1980
- Chemical probes for higher-order structure in RNA.Proceedings of the National Academy of Sciences, 1980
- Ligand-Induced Conformational Changes in Ribonucleic AcidsPublished by Elsevier ,1980
- Chemical Evidence for a Codon‐Induced Allosteric Change in tRNALys Involving the 7‐Methylguanosine Residue 46European Journal of Biochemistry, 1979
- Reactions at the termini of tRNA with T4 RNA ligaseNucleic Acids Research, 1978
- Chemical evidence for a codon‐induced change of tRNA conformationFEBS Letters, 1978
- Studies on polypeptide elongation factors from Escherichia coli. II. Purification of factors Tu-guanosine diphosphate, Ts, and Tu-Ts, and crystallization of Tu-guanosine diphosphate and Tu-Ts.1972
- Initiation of protein synthesis II a convenient assay for the ribosome-dependent synthesis of N-formyl-C14-methionylpuromycinBiochemical and Biophysical Research Communications, 1966
- The synthesis of N-acetylphenylalanyl-sRNABiochemical and Biophysical Research Communications, 1966