Abstract
Abstract Several polynucleotides were reacted with N-acetoxy-N-2-acetylaminofluorene, repurified, and their base compositions analyzed after ribonuclease T2 digestion. This led to the binding of N-2-acetylaminofluorene at the position 8 of guanosine residues in the valine codon, G-U-U, the lysine codon, A-A-G, and in poly(U3,G). This modification completely inactivated the ability of the triplets to stimulate ribosomal binding of their respective aminoacyl transfer RNAs. No miscoding was observed. The modified poly(U3,G) had decreased activity with 14C-valyl-tRNA, but normal activity with 14C-phenylalanyl-tRNA, in the ribosomal binding assay. Employing the same polymer in a protein-synthesizing system, the incorporation of both 14C-valine and 14C-phenylalanine into polypeptides was inhibited. Evidence was obtained that polymers with modified G residues are bound to ribosomes but that polypeptide chain growth is blocked when translation encounters the modified G residues.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
