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PMID: 5289870 Published · ppublish English Journal Article

A model for protein synthesis involving the intermediate formation of peptidyl-5S RNA.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 68 ·No. 10 ·1971-10-00 ·Pages 2357-60

Raacke ID

Abstract

A model for protein synthesis is proposed in which the donor for the peptide elongation reaction is peptidyl-5S RNA. Space-filling models show that peptide bond formation between peptidyl-5S RNA and aminoacyl-tRNA is eminently feasible from a stereochemical point of view. The peptide is transferred to 5S RNA, while at the same time the deacylated tRNA is exchanged by a new aminoacyl-tRNA acceptor. Two peptidyl transferases are required by the model, both of which have sites for binding the termini of both aminoacyl-tRNA and peptidyl-5S RNA. The model makes detailed predictions about the properties of the transferases.

MeSH Terms
Amino Acid Sequence Chloramphenicol Models, Structural Peptide Biosynthesis Peptide Chain Elongation, Translational Protein Binding Puromycin RNA/biosynthesis RNA Nucleotidyltransferases/metabolism RNA, Transfer/metabolism
Chemicals
Puromycin RNA Chloramphenicol RNA, Transfer RNA Nucleotidyltransferases
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Raacke I D
References (24)
24 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.68.10.2357
Published
1971-10-00
Pages
2357-60
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC389421
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.68.10.2357 PMC Full Text View journal details
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