Summary
We describe experiments here which show that chemical esterification of 5′-adenylic acid (5′-AMP) withN-acetylD-orL-phenylalanine (Ac-D- or Ac-L-Phe) imidazolide occurs principally, if not exclusively, at the 2′ position. Furthermore, in experiments with the formation of the 2′–3′ diester with butyric acid andN-acetyl glycine (Ac-Gly), we found the second esterification was also predominantly at the 2′ position. This means that mixed diesters can be predictably prepared with the positions of the substituents known. The results are consistent with a model for the preferential catalytic synthesis ofL-based peptides via a 2′–3′ diester intermediate of purine monoribonucleotides.
Similar content being viewed by others
References
Fraser TH, Rich A (1975) Amino acids are not initially attached to the same position on tRNA molecules. Proc Natl Acad Sci USA 72:3044–3048
Gottikh BP, Krayevsky AA, Tarussova NB, Purygin PP, Tsilvevich TL (1970) The general synthetic route to amino acid esters of nucleosides and nucleoside-5′-triphosphates and some properties of these compounds. Tetrahedron 26:4419–4433
Krayevsky AA, Degterev EV, Gottikh BP, Nikolenko LN (1971) Aminoacyl derivatives of nucleosides, nucleotides, and polynucleotides. 10. Possible use of diethyl phosphate imidazolide for the synthesis of 3′ (2′)-O-aminoacyl nucleotides. Izv Akad Nauk SSSR, Ser Khim 8:1730–1736
Lacey JC Jr, Mullins DW Jr (1983) Experimental studies on the origin of the genetic code, a review. Origins Life 13:1–42
Lacey JC Jr, Weber AL, White WE Jr (1975) Coevolution of the genetic code and the process of protein synthesis. Origins Life 6:273–284
Lacey JC Jr, Seneratne N, Mullins DW Jr (1984) Hydrolytic properties of phenylalanyl- andN-acetylphenylalanyl adenylate anhydrides. Origins Life 15:45–54
Lacey JC Jr, Hall LM, Mullins DW Jr, Watkins CL (1985) Chirally selective, intramolecular interactions observed in an aminoacyl adenylate anhydride. Origins Life 16:151–156
Lacey JC Jr, Mullins DW Jr, Watkins CL (1986) Aliphatic amino acid side chains associate with the “face” of the adenine ring. J Biomol Struct Dyn 3:783–793
Lacey JC Jr, Hawkins AF, Thomas RD, Watkins CL (1988) Differential distribution ofD-andL-amino acids between the 2′ and 3′ positions of the AMP residue at the 3′ terminus of tRNA. Proc Natl Acad Sci USA 85:4996–5000
Lacey JC Jr, Thomas RD, Staves MP, Minic VS, Watkins CL (1989) Purine monoribonucleotides may preferentially catalyze the synthesis ofL-amino acid peptides. Presented at the sixth meeting of the International Society for the Study of the Origin of Life and the ninth International Conference on the Origin of Life, Prague, Czechoslovakia, July 1989. (Abstract) Origins Life Evol Biosphere 19:332–333
Mullins DW Jr, Lacey JC Jr (1986) Comparative rates of esterifications of 5′-AMP with hydrophobic amino acids: relevance to genetic code assignments. J Mol Evol 23:76–79
Paecht-Horowitz M, Eirich FR (1988) Polymerization of amino acid adenylates on sodium montmorillanite with preabsorbed polypeptides. Origins Life Evol Biosphere 18:359–387 (and references therein)
Profy AT, Usher DA (1984) Stereoselective aminoacylation of a dinucleoside monophosphate by the imidazolides ofDl-alanine andN-(tert-butoxycarbonyl)-Dl-alanine. J Mol Evol 20:147–156
Sprinzl M, Cramer F (1979) The-C-C-A end of tRNA and its role in protein synthesis. Prog Nucleic Acid Res Mol Evol 11:189–198
Taiji M, Yokoyama S, Miyazawa T (1983) Transacylation rates of (aminoacyl) adenosine moiety at the 3′ terminus of aminoacyl-tRNA. Biochemistry 22:3220–3225
Taiji M, Yakoyama S, Miyazawa T (1985) Slow transacylation of peptidyl adenosine allows analysis of 2′/3′ isomer specificity of peptidyl transferase. Biochemistry 24:5776–5780
Weber AL, Orgel LE (1978) The formation of peptides from 2′(3′)-glycyl ester of a nucleotide. J Mol Evol 11:189–198
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Lacey, J.C., Thomas, R.D., Wickaramasinghe, N.S. et al. Chemical esterification of 5′-AMP occurs predominantly at the 2′ position. J Mol Evol 31, 251–256 (1990). https://doi.org/10.1007/BF02101120
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/BF02101120