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PMID: 4551981 Published · ppublish English Journal Article

Peptidyl-puromycin synthesis on polyribosomes from Escherichia coli.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 69 ·No. 3 ·1972-03-00 ·Pages 624-8

Pestka S

Abstract

Peptide bond synthesis was studied with native polyribosomes of E. coli. With the use of this system for transpeptidation, it was possible to show that a single K(+) activates the ribosome monomers of polyribosomes; that protonation of a single group (probably imidazole or an N-terminal amino group) with a pK(a) equal to about 7.2 inactivates the transpeptidase complex; that Mn(++) can substitute for Mg(++), but that Ca(++), spermidine, and putrescine do so only very poorly; and that the K(m) for puromycin in this system is about 2.4 x 10(-6) M.

MeSH Terms
Ammonia/pharmacology Autoradiography Escherichia coli/metabolism Hydrogen-Ion Concentration Kinetics Lithium/pharmacology Magnesium/pharmacology Peptide Biosynthesis Peptides/analysis Potassium/pharmacology Protein Binding Puromycin/metabolism Ribosomes/metabolism Sodium/pharmacology Temperature Tritium
Chemicals
Peptides Tritium Puromycin Ammonia Lithium Sodium Magnesium Potassium
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Pestka S
References (23)
23 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.69.3.624
Published
1972-03-00
Pages
624-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC426521
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.69.3.624 PMC Full Text View journal details
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