The Template Theory and the Role of Transpeptidation in Protein Biosynthesis

• Published in: Nature (London) 1953-06, Vol.171 (4362), p.1027-1028
• Main Author: DALGLIESH, C. E
• Format: Article
• Language: English
• Subjects: Humanities and Social Sciences; letter; multidisciplinary; Old Medline; Protein Biosynthesis; Proteins - metabolism; Science; Science (multidisciplinary)
• ISSN: 0028-0836; 1476-4687
• DOI: 10.1038/1711027a0

The synthesis of protein occurs without detectable evidence of free peptide intermediates. This fact, and the specificity of proteins, have been explained by the so-called ‘template theory’, in which it is assumed that the amino-acids are laid down in their correct order on a template (? consisting of nucleic acid) with subsequent bond formation and separation from the template 1 . Recent work has shown that transpeptidation occurs with peptides in artificial systems 2 , and evidence has been sought for the participation of transpeptidation in protein synthesis. In these experiments protein synthesis has been brought about in the presence of isotopically labelled amino-acid. The resultant protein is degraded, the appropriate amino-acid isolated from two different parts of the chain and the specific activities compared. It is assumed that if thetemplate theory is correct, all amino-acids must be laid down on the template effectively simultaneously, so that differences in activity of the same amino-acid residue in different parts of the chain are evidence for transpeptidation 3 . We wish to show that this assumption is not necessarily justifiable.