Structure and Function of E. coli Formylmethionyl tRNA, I. Effect of Modification of Pyrimidine Residues on Aminoacyl Synthetase Recognition*

  1. LaDonne H. Schulman
  1. DEPARTMENT OF DEVELOPMENTAL BIOLOGY AND CANCER, DIVISION OF BIOLOGY, ALBERT EINSTEIN COLLEGE OF MEDICINE, BRONX, NEW YORK

Abstract

E. coli formylmethionyl tRNA (tRNAfMet) has been irradiated with ultraviolet light in the presence of Mg2+ 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 tRNAfMet is due almost entirely to modification of the cytidine residues in the 3′-terminal CCA—OH sequence.

Footnotes

  • Research Career Development awardee (grant 1 KO4 GM 25161 from the National Institute of General Medical Sciences).

  • * This work was supported by research grants from the National Institutes of Health, USPHS (1 RO1 GM 16995), and the American Cancer Society (P-570).

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