Chain Initiation Factor 2

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Formation and release of eukaryotic initiation factor 2 X GDP complex during eukaryotic ribosomal polypeptide chain initiation complex formation.

The formation and release of an eukaryotic initiation factor (eIF)-2 X GDP binary complex during eIF-5-mediated assembly of an 80 S ribosomal polypeptide chain initiation complex have been studied by sucrose gradient centrifugation analysis. Isolated 40 S initiation complex reacts with eIF-5 and 60 S ribosomal subunits to form an 80 S ribosomal initiation complex with concomitant hydrolysis of ...

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Polypeptide chain initiation in eukaryotes: initiation factor MP in Artemia salina embryos.

The activity of IF-MP, a polypeptide chain initiation factor that forms a ternary complex with eukaryotic initiator Met-tRNA and GTP and promotes binding of the initiator to 40S ribosomes, is very low in undeveloped Artemia salina embryos but increases over 20-fold following resumption of development upon hydration of the cysts. The factor is present in both the ribosomal salt wash and high-sp...

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Polypeptide chain initiation in eukaryotes: initiation factor requirements for translation of natural messengers.

A protein-synthesizing system consisting of ribosomes and supernatant of undeveloped Artemia saline embryos is used for assay of mRNA translation and initiation factors. This system contains the components needed for chain elongation but has low levels of mRNA and initiation factors. Exogenous mRNA is readily translated upon addition of high-speed supernatant or ribosomal salt wash of developin...

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Thiostrepton inhibition of initiation factor 1 activity in polypeptide chain initiation in Escherichia coli.

Thiostrepton, a peptide antibiotic, inhibits the GTP-dependent 70S initiation complex formation (as measured by binding of fMet-tRNA to ribosomes and concomitant hydrolysis of GTP) only when initiation factor 1 is present to permit catalytic recycling of initiation factor 2 in the initiation reaction. When initiation factor 1 is absent, the binding of fMet-tRNA and GTP hydrolysis occur stoichio...

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Activity of protein phosphatases against initiation factor-2 and elongation factor-2.

The protein phosphatases active against phosphorylase a, elongation factor-2 (EF-2) and the alpha-subunit of initiation factor-2 (eIF-2) [eIF-2(alpha P)] were studied in extracts of rabbit reticulocytes. Swiss-mouse 3T3 fibroblasts and rat hepatocytes, by use of the specific phosphatase inhibitors okadaic acid and inhibitor proteins-1 and -2. In all three extracts tested, both phosphatase-1 and...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1973

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(19)44374-3