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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Published in | FEBS letters Vol. 153; no. 1; pp. 119 - 124 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
01.01.1983
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Online Access | Get full text |
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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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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 content type line 23 ObjectType-Feature-1 |
ISSN: | 0014-5793 |