Translational machinery and protein folding: Evidence of conformational variants of the estrogen receptor alpha

Research output: Contribution to journalArticle


As an approach to understand how translation may affect protein folding, we analyzed structural and functional properties of the human estrogen receptor alpha synthesized by different eukaryotic translation systems. A minimum of three conformations of the receptor were detected using limited proteolysis and a sterol ligand-binding assay. The receptor in vitro translated in rabbit reticulocyte lysate was rapidly degraded by protease, produced major bands of about 34 kDa and showed a high affinity for estradiol. In a wheat germ translation system, the receptor was more slowly digested. Two soluble co-existing conformations were evident by different degradation patterns and estradiol binding. Our data show that differences in the translation machinery may result in alternative conformations of the receptor with distinct sterol binding properties. These studies suggest that components of the cellular translation machinery itself might influence the protein folding pathways and the relative abundance of different receptor conformers. (C) 2007 Published by Elsevier Inc.


  • Sofia Horjales
  • German Cota
  • Mario Senorale-Pose
  • Carlos Rovira
  • Estela Roman
  • Nora Artagaveytia
  • Ricardo Ehrlich
  • Monica Marin
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Cancer and Oncology


  • wheat germ extract, rabbit reticulocyte lysate, in vitro translation, estrogen receptor, limited proteolysis, in vivo protein folding, protein biosynthesis
Original languageEnglish
Pages (from-to)139-143
JournalArchives of Biochemistry and Biophysics
Issue number2
Publication statusPublished - 2007
Publication categoryResearch