Efficient translation and polyribosome binding of super(125)I-labelled rabbit globin messenger ribonucleoprotein

Rabbit polyribosomal globin messenger ribonucleoprotein (mRNP) was labelled under mild conditions, using super(125)I and Iodogen, in the protein moiety so that the fate of mRNA-associated protein could be followed during translation. super(125)I-mRNP was shown to retain functional activity in the nu...

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Bibliographic Details
Published inFEBS letters Vol. 153; no. 1; pp. 119 - 124
Main Authors Butcher, P D, Arnstein, HRV
Format Journal Article
LanguageEnglish
Published 01.01.1983
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Summary:Rabbit polyribosomal globin messenger ribonucleoprotein (mRNP) was labelled under mild conditions, using super(125)I and Iodogen, in the protein moiety so that the fate of mRNA-associated protein could be followed during translation. super(125)I-mRNP was shown to retain functional activity in the nuclease-treated reticulocyte lysate translation system under optimal labelling conditions. Polyribsome binding of super(125)I-mRNP and its sensitivity to cycloheximide indicated a functional-and translation-dependent binding of mRNP proteins. The results constitute a successful and direct approach to the study of mRNA-associated proteins in translational control.
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ISSN:0014-5793