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Efficient translation and polyribosome binding of 125 I‐labelled rabbit globin messenger ribonucleoprotein
Author(s) -
Butcher P.D.,
Arnstein H.R.V.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80130-6
Subject(s) - reticulocyte , polysome , ribonucleoprotein , translation (biology) , messenger rna , globin , cycloheximide , messenger rnp , protein biosynthesis , biochemistry , biology , chemistry , microbiology and biotechnology , ribosome , rna , gene
Rabbit polyribosomal globin messenger ribonucleoprotein (mRNP) was labelled under mild conditions, using 125 I and Iodogen, in the protein moiety so that the fate of mRNA‐associated proteins could be followed during translation. 125 I‐mRNP was shown to retain functional activity in the nuclease‐treated reticulocyte lysate translation system under optimal labelling conditions. Polyribosome binding of 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.