The translational capacity of deadenylated ovalbumin messenger RNA.
We present evidence that the poly(A) sequence at the 3' end of ovalbumin mRNA has an effect on its translational efficiency in a reticulocyte lysate cell-free system. Polynucleotide phosphorylase has been used to remove selectively the poly(A) while leaving the rest of the molecule intact. It is shown that the stability of the mRNA in a cell free system is not appreciably affected by this procedure. Measurements of the size of ovalbumin-synthesizing polysomes, rate of peptide elongation, and number of rounds of translation per messenger show a generally reduced efficiency for deadenylated mRNA compared to native mRNA. No comparable difference was observed in experiments with a wheat germ cell-free system, which gives few rounds of translation per mRNA. This indicates that the effect results from a lowering of the efficiency of reinitiation on deadenylated mRNA.
D001483:Base Sequence; D002474:Cell-Free System; D010047:Ovalbumin / Q000096:biosynthesis*; D011061:Poly A / Q000378:metabolism*; D011132:Polyribosomes / Q000378:metabolism; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000378:metabolism*
D012333:RNA, Messenger; D011061:Poly A; D010047:Ovalbumin