Open AccessStructure investigation of Phe-tRNAphefromE.colibound to the ribosomal A-site
Author(s) -
Sabine Bertram,
Ulrich Göringer,
Rolf Wagner
Publication year - 1983
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/11.3.575
Subject(s) - biology , transfer rna , ribosomal rna , escherichia coli , ribosome , genetics , microbiology and biotechnology , rna , gene
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 modification of G-34 at the anticodon loop triggers a conformational instability in distant parts of the tRNA molecule.