Translational machinery and protein folding: Evidence of conformational variants of the estrogen receptor alpha
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/969324
- author
- Horjales, Sofia ; Cota, German ; Senorale-Pose, Mario ; Rovira, Carlos LU ; Roman, Estela ; Artagaveytia, Nora ; Ehrlich, Ricardo and Marin, Monica
- organization
- publishing date
- 2007
- 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
- 2016-04-01 12:13:23
- date last changed
- 2022-01-27 00:38:36
@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}}, keywords = {{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}}, doi = {{10.1016/j.abb.2007.07.029}}, volume = {{467}}, year = {{2007}}, }