Chain Initiation and Control of Protein Synthesis
- 11 March 1966
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 151 (3715) , 1241-1245
- https://doi.org/10.1126/science.151.3715.1241
Abstract
Analysis of the enzymatic mechanism of chain extension during protein synthesis and studies with N-formylmethionyl-sRNA suggest that chain initiation requires formylation of the amino group of the amino acid destined to start chain growth. The existence of a set of starting triplets coding for a special set of N-formylaminoacyl-sRNA's is postulated. These triplets might be ambiguous in the sense that they specify different amino acids, depending on whether they are at the beginning of or within a message. A number of starting triplets and their NH2-terminal amino acids are predicted from previously suggested ambiguities. The biochenmical, regulatory, and genetic implications of a formylation step controlling chain initiation are discussed.This publication has 28 references indexed in Scilit:
- The formation of N-formyl-methionyl-sRNAJournal of Molecular Biology, 1965
- Gramicidin A. V. The Structure of Valine- and Isoleucine-gramicidin AJournal of the American Chemical Society, 1965
- Binding of transfer ribonucleic acid to ribosomes engaged in protein synthesis: Number and properties of ribosomal binding sitesJournal of Molecular Biology, 1965
- Role of the Genetic Message in Initiation and Release of the Polypeptide ChainNature, 1964
- Structure and Function of E. Coli ErgosomesNature, 1963
- Ribosomal Aggregates Engaged in Protein Synthesis : Ergosome Breakdown and Messenger Ribonucleic Acid TransportNature, 1963
- Polypeptide synthesis in Escherichia coliJournal of Molecular Biology, 1963
- Hemoglobin FI, an acetyl-containing hemoglobinBiochimica et Biophysica Acta, 1962
- The protein subunit of turnip yellow mosaic virusJournal of Molecular Biology, 1961
- Isolation of acetylpeptide from enzymic digests of TMV-proteinBiochimica et Biophysica Acta, 1958