EF-1 alpha is a target site for an inhibitory effect of quercetin in the peptide elongation process.

  • C Marcinkiewicz Department of General and Organic Chemistry, Medical Academy, Białystok, Poland.;
  • W Gałasiński
  • A Gindzieński

Abstract

The effect of quercetin (3,3',4',5,7-pentahydroxyflavone) on the polypeptide elongation system isolated from rat liver cells, was investigated. Quercetin inhibited [14C]leucine incorporation into proteins in vitro and the inhibitory effect is being directed towards the elongation factor eEF-1, but not to eEF-2 and ribosomes. Quercetin was found to form a complex with EF-1 alpha, which was inactive in GTP-dependent binding to ribosomes. It can be suggested that quercetin can block the total or the part of the domain of EF-1 alpha structure that is responsible for formation of the ternary complex EF-1 alpha-GTP-[14C]Phe-tRNA and therefore preventing formation of the quaternary complex with ribosomes.
Published
1995-09-30
Section
Articles