z-logo
open-access-imgOpen Access
Structure and Function of E. coli Formylmethionyl tRNA, I. Effect of Modification of Pyrimidine Residues on Aminoacyl Synthetase Recognition
Author(s) -
LaDonne H. Schulman
Publication year - 1970
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.66.2.507
Subject(s) - transfer rna , cytidine , uridine , aminoacylation , ultraviolet light , biochemistry , escherichia coli , methionine , pyrimidine , chemistry , amino acid , biology , rna , stereochemistry , enzyme , photochemistry , gene
E. coli formylmethionyl tRNA (tRNA(fMet)) has been irradiated with ultraviolet light in the presence of Mg(2+) to the extent of 50 per cent inactivation of amino acid acceptance. Separation of active and inactive molecules after irradiation has shown that ultraviolet light modification of the uridine in the anticodon, the uridine in the small loop, the 4-thiouridine, and the pyrimidines in the double-stranded stem adjacent to the dihydrouridine loop has no effect on aminoacylation or transformylation. The ultraviolet light-induced inactivation of methionine acceptance by tRNA(fMet) is due almost entirely to modification of the cytidine residues in the 3'-terminal CCA-OH sequence.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom