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Amino acid esters of 9-(2′,3′-dihydroxypropyl-1′)-adenine are the specific inhibitors of protein synthesis on ribosomes

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Abstract

Peptide acceptor properties of phenylalanine and glycine esters of 9′-(2′,3′-dihydroxypropyl-1′)-adenine and 1-(2′,3′-dihydroxypropyl-1′)-4-thiouracyl were investigated. All these esters appeared to be powerful inhibitors of polyphenylalanine synthesis in E. coli MRE-600 ribosomes charged with poly U. Like puromycin, esters of adenine derivatives accepted the AcPhe residue from Ac-[14C] Phe-tRNA in a ribosomal system charged with poly U. However, peptidyl esters of 9-(2′,3′-dihydroxypropyl-1′)-adenine remained bound with ribosomes. The structure of the peptide esters synthesized was ascertained after dissociation of ribosomes into subparticles by direct comparison with the synthetic specimens.

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Abbreviations

AcPhe:

acetyl-l-phenylalanine

HP-Ade:

9-(2′,3′-dihydroxypropyl-1′)-adenine

Phe-HP-Ade and Gly-HP-Ade:

l-phenylalanine and glycine esters of HP-Ade

Phe-HP-TUra:

l-phenylalanine ester 1-(2′,3′-dihydroxypropyl-1′)-4-thiouracyl

AcPhePhe-HP-Ade and AcPheGly-HP-Ade:

acetyl-l-diphenylalanine and acetyl-l-phenylalanylglycine esters of HP-Ade respectively

AcPhe-puromycin:

acetyl-l-phenylalanyl-puromycin

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Gottikh, B.P., Krayevsky, A.A., Kukhanova, M.K. et al. Amino acid esters of 9-(2′,3′-dihydroxypropyl-1′)-adenine are the specific inhibitors of protein synthesis on ribosomes. Molecular Biology Reports 1, 173–178 (1973). https://doi.org/10.1007/BF00357159

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  • DOI: https://doi.org/10.1007/BF00357159

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