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

Horjales, Sofia; Cota, German; Senorale-Pose, Mario; Rovira, Carlos LU ; Roman, Estela; Artagaveytia, Nora; Ehrlich, Ricardo and Marin, Monica (2007) In Archives of Biochemistry and Biophysics 467(2). p.139-143
Abstract
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... (More)
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. (Less)
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organization
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type
Contribution to journal
publication status
published
subject
keywords
wheat germ extract, rabbit reticulocyte lysate, in vitro translation, estrogen receptor, limited proteolysis, in vivo protein folding, protein biosynthesis
in
Archives of Biochemistry and Biophysics
volume
467
issue
2
pages
139 - 143
publisher
Academic Press
external identifiers
  • wos:000251067100001
  • scopus:35748967314
ISSN
0003-9861
DOI
10.1016/j.abb.2007.07.029
language
English
LU publication?
yes
id
8724aa45-c8ee-4552-8485-821711cebdc1 (old id 969324)
date added to LUP
2008-01-29 15:33:27
date last changed
2017-11-05 03:41:25
@article{8724aa45-c8ee-4552-8485-821711cebdc1,
  abstract     = {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.},
  author       = {Horjales, Sofia and Cota, German and Senorale-Pose, Mario and Rovira, Carlos and Roman, Estela and Artagaveytia, Nora and Ehrlich, Ricardo and Marin, Monica},
  issn         = {0003-9861},
  keyword      = {wheat germ extract,rabbit reticulocyte lysate,in vitro translation,estrogen receptor,limited proteolysis,in vivo protein folding,protein biosynthesis},
  language     = {eng},
  number       = {2},
  pages        = {139--143},
  publisher    = {Academic Press},
  series       = {Archives of Biochemistry and Biophysics},
  title        = {Translational machinery and protein folding: Evidence of conformational variants of the estrogen receptor alpha},
  url          = {http://dx.doi.org/10.1016/j.abb.2007.07.029},
  volume       = {467},
  year         = {2007},
}