Peptidyl-puromycin synthesis on polyribosomes from Escherichia coli.
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Journal: 1972/May - Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
PUBMED: 4551981
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.
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Proc Natl Acad Sci U S A 69(3): 624-628
PMID: 4551981

Peptidyl-Puromycin Synthesis on Polyribosomes from <em>Escherichia coli</em><sup><a href="#fn1" rid="fn1" class=" fn">*</a></sup>

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 pKa 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 Km for puromycin in this system is about 2.4 × 10 M.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.
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Roche Institute of Molecular Biology, Nutley, New Jersey 07110
This paper is no. XVIII in the series, Studies on Transfer Ribonucleic Acid-Ribosome Complexes. The preceding publication in this series is listed as ref. 1.
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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 pKa 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 Km for puromycin in this system is about 2.4 × 10 M.
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