Purification and properties of rabbit reticulocyte elongation factor

Kemper, Wayne M.; Merrick, William C.; Redfield, Betty; Liu, Chen Kao; Weissbach, Herbert

doi:10.1016/0003-9861(76)90389-1

Cited by 96 publications

(66 citation statements)

References 30 publications

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“…The translation factor eIF5A was originally identified as an initiation factor based on its ability to promote methionylpuromycin synthesis (Kemper et al 1976;Schreier et al 1977;, an in vitro assay designed to monitor first peptide bond synthesis. However, this assay also monitors the peptidyl-transferase activity of the ribosome.…”

Section: Eif5a Promotion Of Peptide Bond Formationmentioning

confidence: 99%

Mechanism and Regulation of Protein Synthesis in Saccharomyces cerevisiae

2016

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In this review, we provide an overview of protein synthesis in the yeast Saccharomyces cerevisiae. The mechanism of protein synthesis is well conserved between yeast and other eukaryotes, and molecular genetic studies in budding yeast have provided critical insights into the fundamental process of translation as well as its regulation. The review focuses on the initiation and elongation phases of protein synthesis with descriptions of the roles of translation initiation and elongation factors that assist the ribosome in binding the messenger RNA (mRNA), selecting the start codon, and synthesizing the polypeptide. We also examine mechanisms of translational control highlighting the mRNA cap-binding proteins and the regulation of GCN4 and CPA1 mRNAs.

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Section: Eif5a Promotion Of Peptide Bond Formationmentioning

confidence: 99%

Mechanism and Regulation of Protein Synthesis in Saccharomyces cerevisiae

2016

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“…Eukaryotic translation initiation factor 5A (eIF5A) was isolated from ribosome of rabbit reticulocyte extracts in 1976 (Kemper et al, 1976). Its denomination derived from the in vitro observation for its stimulatory effect on synthesis of methionyl-puromycin, an assay used to evaluate factors involved in the first peptide bond (Benne and Hershey, 1978;Park et al, 1993).…”

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confidence: 99%

Involvement of eukaryotic translation initiation factor 5A (eIF5A) in skeletal muscle stem cell differentiation

Luchessi

Cambiaghi

Hirabara

et al. 2008

Journal Cellular Physiology

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The eukaryotic translation initiation factor 5A (eIF5A) contains a special amino acid residue named hypusine that is required for its activity, being produced by a post-translational modification using spermidine as substrate. Stem cells from rat skeletal muscles (satellite cells) were submitted to differentiation and an increase of eIF5A gene expression was observed. Higher content of eIF5A protein was found in satellite cells on differentiation in comparison to non-differentiated satellite cells and skeletal muscle. The treatment with N1-guanyl-1,7-diaminoheptane (GC7), a hypusination inhibitor, reversibly abolished the differentiation process. In association with the differentiation blockage, an increase of glucose consumption and lactate production and a decrease of glucose and palmitic acid oxidation were observed. A reduction in cell proliferation and protein synthesis was also observed. L-Arginine, a spermidine precursor and partial suppressor of muscle dystrophic phenotype, partially abolished the GC7 inhibitory effect on satellite cell differentiation. These results reveal a new physiological role for eIF5A and contribute to elucidate the molecular mechanisms involved in muscle regeneration.

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“…They occur in calf brain (Legocki et al, 1974) and also in rabbit reticulocytes (Kemper et al, 1976). All these multiple forms seem to have a comparable functional activity and efficiently translate synthetic polynucleotides (Kemper et al, 1976). On the contrary, peptide-elongation activity present in our fraction C is unable to translate artificial templates, although it is very active with polyribosomes.…”

Section: Discussionmentioning

confidence: 91%

“…Multiple forms of EF 1 have been repeatedly reported during the past years. They occur in calf brain (Legocki et al, 1974) and also in rabbit reticulocytes (Kemper et al, 1976). All these multiple forms seem to have a comparable functional activity and efficiently translate synthetic polynucleotides (Kemper et al, 1976).…”

Section: Discussionmentioning

confidence: 99%

All factors required for protein synthesis are retained on heparin bound to Sepharose

Hradec¹,

Dusek²

1978

Biochemical Journal

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1. Postmitochondrial supernatants ofrabbit reticulocyte lysates were chromatographed on heparin bound to Sepharose 4B, and the fraction retained on affinity columns was separated by subsequent gel filtration on Sepharose 4B into three fractions, two of them active in protein synthesis. 2. The heavier fraction sedimented at 40 S and contained more than 10% RNA. This consisted predominantly of a 12S component, with smaller amounts of the 9S and 4S RNA species. The lighter fraction (18-20S) was composed of proteins with less than 1 % RNA. 3. Different enzymic activities were associated with these fractions. 4. In the presence of both fractions, efficient translation took place on combined ribosomal subunits of rat liver with added cofactors. Globin messenger ribonucleoprotein stimulated this translation 5-6-fold. 5. Relatively large complexes of all factors required for protein synthesis are apparently isolated from reticulocytes by affinity chromatography on heparin-Sepharose 4B. Such complexes may occur naturally in the cytoplasm of mammalian cells.

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Purification and properties of rabbit reticulocyte elongation factor

Cited by 96 publications

References 30 publications

Mechanism and Regulation of Protein Synthesis in Saccharomyces cerevisiae

Mechanism and Regulation of Protein Synthesis in Saccharomyces cerevisiae

Involvement of eukaryotic translation initiation factor 5A (eIF5A) in skeletal muscle stem cell differentiation

All factors required for protein synthesis are retained on heparin bound to Sepharose

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