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PMID: 4554533 Published · ppublish English Journal Article

Covalent attachment of a peptidyl-transfer RNA analog to the 50S subunit of Escherichia coli ribosomes.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 69 ·No. 4 ·1972-04-00 ·Pages 837-41

Pellegrini M, Oen H, Cantor CR

Abstract

The peptidyl-tRNA analog, N-bromo-acetyl-Phenylalanyl-tRNA(Phe) has been prepared. Its binding to the 70S ribosome of E. coli is totally dependent upon polyuridylic acid. The analog becomes covalently attached to the 50S particle. It is associated with only one protein fraction after polyacrylamide-gel separation of total 50S proteins. The analog also reacts with 23S ribosomal RNA or a protein that remains tightly bound to this RNA after treatment with LiCl-urea and sodium dodecyl sulfate. The analog can function as a peptidyl-tRNA for at least one peptide transfer, but it then inhibits further chain elongation. This result strongly suggests that this analog becomes covalently bound at the P-site of the ribosome.

MeSH Terms
Acetates/chemical synthesis,metabolism Acrylamides Binding Sites Bromine Centrifugation, Density Gradient Escherichia coli/metabolism Peptide Chain Elongation, Translational/drug effects Peptides/chemical synthesis,metabolism Phenylalanine/chemical synthesis,metabolism Polynucleotides/pharmacology Protein Binding/drug effects RNA, Bacterial/metabolism RNA, Transfer/chemical synthesis,metabolism Ribosomes/metabolism Sodium Dodecyl Sulfate/pharmacology Uracil Nucleotides/pharmacology Urea/pharmacology
Chemicals
Acetates Acrylamides Peptides Polynucleotides RNA, Bacterial Uracil Nucleotides Sodium Dodecyl Sulfate Phenylalanine Urea RNA, Transfer Bromine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Pellegrini M
Oen H
Cantor C R
References (20)
20 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.69.4.837
Published
1972-04-00
Pages
837-41
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC426576
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.69.4.837 PMC Full Text View journal details
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