Defective 30S ribosomal particles in a polyamine auxotroph of Escherichia coli
Polypeptide synthesis directed by poly(U) or MS 2 phage RNA is several fold more active in cell-free systems prepared from polyamine supplemented bacteria than in extracts of polyamine depleted cells. This effect depends on the presence of defective 30S ribosomal subunits in the starved bacteria. It...
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todo:paper_0006291X_v67_n3_p1185_Echandi2023-10-03T14:04:09Z Defective 30S ribosomal particles in a polyamine auxotroph of Escherichia coli Echandi, G. Algranati, I.D. polyamine putrescine auxotrophic mutant escherichia coli in vitro study microorganism protein synthesis ribosome theoretical study Escherichia coli Kinetics Magnesium Peptide Synthesis Poly U Polyamines Putrescine Ribosomes RNA, Viral Spermidine Translation, Genetic Polypeptide synthesis directed by poly(U) or MS 2 phage RNA is several fold more active in cell-free systems prepared from polyamine supplemented bacteria than in extracts of polyamine depleted cells. This effect depends on the presence of defective 30S ribosomal subunits in the starved bacteria. It is concluded that polyamines play a role in the normal biosynthesis, maturation and/or assembly of the small ribosomal subparticles. © 1975. Fil:Algranati, I.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_0006291X_v67_n3_p1185_Echandi |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
polyamine putrescine auxotrophic mutant escherichia coli in vitro study microorganism protein synthesis ribosome theoretical study Escherichia coli Kinetics Magnesium Peptide Synthesis Poly U Polyamines Putrescine Ribosomes RNA, Viral Spermidine Translation, Genetic |
spellingShingle |
polyamine putrescine auxotrophic mutant escherichia coli in vitro study microorganism protein synthesis ribosome theoretical study Escherichia coli Kinetics Magnesium Peptide Synthesis Poly U Polyamines Putrescine Ribosomes RNA, Viral Spermidine Translation, Genetic Echandi, G. Algranati, I.D. Defective 30S ribosomal particles in a polyamine auxotroph of Escherichia coli |
topic_facet |
polyamine putrescine auxotrophic mutant escherichia coli in vitro study microorganism protein synthesis ribosome theoretical study Escherichia coli Kinetics Magnesium Peptide Synthesis Poly U Polyamines Putrescine Ribosomes RNA, Viral Spermidine Translation, Genetic |
description |
Polypeptide synthesis directed by poly(U) or MS 2 phage RNA is several fold more active in cell-free systems prepared from polyamine supplemented bacteria than in extracts of polyamine depleted cells. This effect depends on the presence of defective 30S ribosomal subunits in the starved bacteria. It is concluded that polyamines play a role in the normal biosynthesis, maturation and/or assembly of the small ribosomal subparticles. © 1975. |
format |
JOUR |
author |
Echandi, G. Algranati, I.D. |
author_facet |
Echandi, G. Algranati, I.D. |
author_sort |
Echandi, G. |
title |
Defective 30S ribosomal particles in a polyamine auxotroph of Escherichia coli |
title_short |
Defective 30S ribosomal particles in a polyamine auxotroph of Escherichia coli |
title_full |
Defective 30S ribosomal particles in a polyamine auxotroph of Escherichia coli |
title_fullStr |
Defective 30S ribosomal particles in a polyamine auxotroph of Escherichia coli |
title_full_unstemmed |
Defective 30S ribosomal particles in a polyamine auxotroph of Escherichia coli |
title_sort |
defective 30s ribosomal particles in a polyamine auxotroph of escherichia coli |
url |
http://hdl.handle.net/20.500.12110/paper_0006291X_v67_n3_p1185_Echandi |
work_keys_str_mv |
AT echandig defective30sribosomalparticlesinapolyamineauxotrophofescherichiacoli AT algranatiid defective30sribosomalparticlesinapolyamineauxotrophofescherichiacoli |
_version_ |
1807318374553747456 |