Journal ArticleDOI
Effects of hemin and other porphyrins on protein synthesis in a reticulocyte lysate cell-free system.
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TLDR
Metal derivatives of protoporphyrin IX have been synthesized and tested for ability to replace hemin in sustaining the rate of protein synthesis in the intact cell and in the lysate system and it is found that the cobalt, nickel, magnesium and zinc derivatives will replace he Min in the LYSate system, whereas the copper derivative will not.About:
This article is published in Journal of Molecular Biology.The article was published on 1969-06-14. It has received 76 citations till now. The article focuses on the topics: Hemin & Protoporphyrin IX.read more
Citations
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Journal ArticleDOI
Regulation of protein synthesis in mammalian cells: II. Inhibition of protein synthesis at the level of initiation during mitosis☆☆☆
Hung Fan,Sheldon Penman +1 more
TL;DR: It appears that the reduced protein synthesis during mitosis results from a lowered rate of attachment of ribosomes to messenger RNA and initiation of polypeptide synthesis.
Journal ArticleDOI
Mapping the cleavage site in protein synthesis initiation factor eIF-4 gamma of the 2A proteases from human Coxsackievirus and rhinovirus.
Barry J. Lamphear,Riqiang Yan,Fang Yang,Debra A. Waters,Hans Dieter Liebig,Hannes Klump,Ernst Kuechler,Tim Skern,Robert E. Rhoads +8 more
TL;DR: This report has used highly purified recombinant 2A protease from either human Coxsackievirus serotype B4 or rhinovirus serotypes 2 to cleave eIF-4 gamma in vitro in the eif-4 complex purified from rabbit reticulocytes, and found neither the rate of cleavage nor fragment sizes were affected by addition of e IF-3.
Journal ArticleDOI
Initiation of protein synthesis: evidence for messenger RNA-independent binding of methionyl-transfer RNA to the 40 S ribosomal subunit.
TL;DR: It is proposed that the first step in the initiation of protein synthesis in the reticuloeyte lysate is the formation of a 40 S/Met-tRNA f complex, which binds mRNA at the correct initiation site and, after joining with a 60 S subunit, an 80 S /mRNA initiation complex is formed.
Journal ArticleDOI
The characteristics of inhibition of protein synthesis by double-stranded ribonucleic acid in reticulocyte lysates.
TL;DR: The results indicate that low levels of dsRNA promote the formation of an inhibitor which may exist in two forms: one that is reversible by high levels ofdsRNA and one which is irreversible.
Book ChapterDOI
The regulation of initiation of mammalian protein synthesis.
TL;DR: It is expected that the development of cell-free protein synthesizing systems from nucleated cells will allow the pursuit of questions about the regulation of initiation of mammalian protein synthesis.
References
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Journal ArticleDOI
Factors affecting the rate of protein synthesis in lysate systems from reticulocytes.
TL;DR: Exogenous hemin increases the extent of de novo synthesis of hemoglobin and, at 28 °, greatly retards disaggregation of polysomes that accompanies protein synthesis in the lysate.
Journal ArticleDOI
Factors affecting protein synthesis in vitro in rabbit reticulocytes.
TL;DR: In order to obtain a maximal rate of protein synthesis the reaction mixture was improved further by adding to it certain substances which depend upon added iron for their effect, which increased the effect of plasma.
Journal ArticleDOI
Hemoglobin synthesis in rabbit reticulocytes in vitro.
Jacques Kruh,Henry Borsook +1 more
TL;DR: The rapid incorporation of labeled amino acids into the proteins of rabbit reticulocytes in vitro and the stimulation of this process by certain amino acids, iron, fructose-amino acids, glucose, and some, as yet, unidentified material in the filtrate of boiled plasma are reported.
Journal ArticleDOI
Control of reticulocyte polyribosome content and hemoglobin synthesis by heme
TL;DR: Results indicate that hemin is the intracellular mediator of polyribosome assembly; the metalloporphyrin in some manner induces the aggregation of monomeric ribosomes and, presumably, messenger RNA into functionalpolyribosomes.
Journal ArticleDOI
Effects of cycloheximide on polyribosome function in reticulocytes.
TL;DR: The results are consistent with the hypothesis that protein synthesis is accompanied by an exchange of ribosome between the polyribosomal aggregates and the pool of single ribosomes, and that the detachment of Ribosomes from the aggregates is slowed by 4 × 10 −6 m -cycloheximide.