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Aurintricarboxylic acid inhibition of the binding of phenylalanyl‐tRNAa to rat liver ribosomal subunits
Author(s) -
Leader David P.
Publication year - 1972
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(72)80055-3
Subject(s) - aurintricarboxylic acid , citation , library science , chemistry , biochemistry , computer science , apoptosis , programmed cell death
Aurintricarboxylic acid (ATA) inhibits the initiation of protein synthesis in cell-free systems from both prokaryotes and eukaryotes at concentrations which do not affect chain elongation [ l-71 . We report here the effect of ATA on the poly U-dependent binding of Phe-tRNA to rat liver ribosomal subunits. ATA inhibits Phe-tRNA binding to 40 S subunits, catalysed by the rat liver cytosol initiation factor Ml (formerly called 40 S binding factor [8,9]). Binding to recombined 40 S and 60 S subunits, catalysed by elongation factor T-I, is inhibited to a similar extent; however, non-enzymic binding to subunits is inhibited to a greater extent. This unexpected differential inhibition appears to be due to the ability of enzymically inactive protein (present in the partially purified factor preparations) to bind ATA, reducing the amount of the latter available for inhibition of the binding of Phe-tRNA to ribosomes.