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Incorporation of Rat‐Liver 40‐S Ribosomal Subparticles into Rabbit‐Reticulocyte Polysomes

Sophia A. Bonanou‐Tzedaki, H. R. V. Arnstein

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Abstract

The attachment of derived 3H‐labelled rat‐liver 40‐S subparticles to haemoglobin mRNA, present in the polysomes of a rabbit‐reticulocyte lysate, has been studied by sucrose‐gradient analysis. The attachment is dependent on time, energy and temperature, is reduced by cycloheximide and abolished by aurintricarboxylic acid. The resulting “hybrid” polysomes appear as active as the endogenous polysomes in protein synthesis. It is concluded that in an unfractionated‐reticulocyte lysate, heterologous 40‐S subparticles may become incorporated into polysomes without any additional factors.

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What this paper is about

The attachment of derived 3H‐labelled rat‐liver 40‐S subparticles to haemoglobin mRNA, present in the polysomes of a rabbit‐reticulocyte lysate, has been studied by sucrose‐gradient analysis. The attachment is dependent on time, energy and temperature, is reduced by cycloheximide and abolished by aurintricarboxylic acid. The resulting “hybrid” polysomes appear as active as the endogenous polysomes in protein synthesis. It is concluded that in an unfractionated‐reticulocyte lysate, heterologous 40‐S subparticles may become incorporated into polysomes without any additional factors.

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Available abstract

The attachment of derived 3H‐labelled rat‐liver 40‐S subparticles to haemoglobin mRNA, present in the polysomes of a rabbit‐reticulocyte lysate, has been studied by sucrose‐gradient analysis. The attachment is dependent on time, energy and temperature, is reduced by cycloheximide and abolished by aurintricarboxylic acid. The resulting “hybrid” polysomes appear as active as the endogenous polysomes in protein synthesis. It is concluded that in an unfractionated‐reticulocyte lysate, heterologous 40‐S subparticles may become incorporated into polysomes without any additional factors.

Key concepts: Polysome, Reticulocyte, Cycloheximide, Aurintricarboxylic acid, Lysis, Heterologous, Ribosome, Protein biosynthesis

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