Efficient translation and polyribosome binding of 125I-labelled rabbit globin messenger ribonucleoprotein.
Rabbit polyribosomal globin messenger ribonucleoprotein (mRNP) was labelled under mild conditions, using 125I and Iodogen, in the protein moiety so that the fate of mRNA-associated proteins could be followed during translation. 125I-mRNP was shown to retain functional activity in the nuclease-treated reticulocyte lysate translation system under optimal labelling conditions. Polyribsome binding of 125I-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.
D000818:Animals; D003513:Cycloheximide / Q000494:pharmacology; D005914:Globins / Q000096:biosynthesis*; D007457:Iodine Radioisotopes; D007553:Isotope Labeling; D008715:Methionine / Q000378:metabolism; D009698:Nucleoproteins / Q000378:metabolism*; D011132:Polyribosomes / Q000187:drug effects / Q000378:metabolism*; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000378:metabolism*; D011817:Rabbits; D012156:Reticulocytes / Q000378:metabolism; D012261:Ribonucleoproteins / Q000378:metabolism*
D007457:Iodine Radioisotopes; D009698:Nucleoproteins; D012333:RNA, Messenger; D012261:Ribonucleoproteins; D005914:Globins; D003513:Cycloheximide; D008715:Methionine