SwePub - search: WFRF:(Artagaveytia Nora)

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1.	Horjales, Sofia, et al. (author) Translational machinery and protein folding: Evidence of conformational variants of the estrogen receptor alpha 2007 In: Archives of Biochemistry and Biophysics. - : Elsevier BV. - 0003-9861. ; 467:2, s. 139-143 Journal article (peer-reviewed)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.

Horjales, Sofia, et al. (author)
Translational machinery and protein folding: Evidence of conformational variants of the estrogen receptor alpha
2007
In: Archives of Biochemistry and Biophysics. - : Elsevier BV. - 0003-9861. ; 467:2, s. 139-143
Journal article (peer-reviewed)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.

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