Assisted protein folding at low temperature: evolutionaryadaptation of the Antarctic fish chaperonin CCT and its clientproteins
Eukaryotic ectotherms of the Southern Ocean face energetic challenges to protein folding assisted by the cytosolic chaperonin CCT. We hypothesize that CCT and its client proteins (CPs) have co-evolved molecular adaptations that facilitate CCT–CP interaction and the ATP-driven folding cycle at low te...
| Autores: | , , , , , , , |
|---|---|
| Tipo de recurso: | artículo |
| Fecha de publicación: | 2014 |
| País: | España |
| Institución: | Universidad de Cantabria (UC) |
| Repositorio: | UCrea Repositorio Abierto de la Universidad de Cantabria |
| Idioma: | inglés |
| OAI Identifier: | oai:repositorio.unican.es:10902/7814 |
| Acceso en línea: | http://hdl.handle.net/10902/7814 |
| Access Level: | acceso abierto |
| Palabra clave: | CCT TriC Chaperone Chaperonin Protein folding Actin Tubulin Thermal adaptation Evolution |
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Assisted protein folding at low temperature: evolutionaryadaptation of the Antarctic fish chaperonin CCT and its clientproteinsCuellar, JorgeYébenes, HugoParker, Sandra K.Carranza Ferrer, Gerardo|||0000-0003-1081-7850Serna, MarinaValpuesta Moralejo, José MaríaZabala Otaño, Juan Carlos|||0000-0003-2679-5473Detrich, H. WilliamCCTTriCChaperoneChaperoninProtein foldingActinTubulinThermal adaptationEvolutionEukaryotic ectotherms of the Southern Ocean face energetic challenges to protein folding assisted by the cytosolic chaperonin CCT. We hypothesize that CCT and its client proteins (CPs) have co-evolved molecular adaptations that facilitate CCT–CP interaction and the ATP-driven folding cycle at low temperature. To test this hypothesis, we compared the functional and structural properties of CCT–CP systems from testis tissues of an Antarctic fish, Gobionotothen gibberifrons (Lo¨nnberg) (habitat/body T=-1.9 to +2˚C), and of the cow (body T=37˚C). We examined the temperature dependence of the binding of denatured CPs (bactin, b-tubulin) by fish and bovine CCTs, both in homologous and heterologous combinations and at temperatures between 24˚C and 20˚C, in a buffer conducive to binding of the denatured CP to the open conformation of CCT. In homologous combination, the percentage of G. gibberifrons CCT bound to CP declined linearly with increasing temperature, whereas the converse was true for bovine CCT. Binding of CCT to heterologous CPs was low, irrespective of temperature. When reactions were supplemented with ATP, G. gibberifrons CCT catalyzed the folding and release of actin at 2˚C. The ATPase activity of apo-CCT from G. gibberifrons at 4˚C was, 2.5-fold greater than that of apo-bovine CCT, whereas equivalent activities were observed at 20˚C. Based on these results, we conclude that the catalytic folding cycle of CCT from Antarctic fishes is partially compensated at their habitat temperature, probably by means of enhanced CP-binding affinity and increased flexibility of the CCT subunits.The Company of Biologists LtdUniversidad de Cantabria20142014-04-15journal articlehttp://purl.org/coar/resource_type/c_6501NAhttp://purl.org/coar/version/c_be7fb7dd8ff6fe43info:eu-repo/semantics/articlehttp://hdl.handle.net/10902/7814Biology Open 2014 Apr 15; 3(4): 261–270reponame:UCrea Repositorio Abierto de la Universidad de Cantabriainstname:Universidad de Cantabria (UC)Inglésengopen accesshttp://purl.org/coar/access_right/c_abf2Atribución 3.0 Españahttp://creativecommons.org/licenses/by/3.0/es/info:eu-repo/semantics/openAccessoai:repositorio.unican.es:10902/78142026-06-02T12:39:31Z |
| dc.title.none.fl_str_mv |
Assisted protein folding at low temperature: evolutionaryadaptation of the Antarctic fish chaperonin CCT and its clientproteins |
| title |
Assisted protein folding at low temperature: evolutionaryadaptation of the Antarctic fish chaperonin CCT and its clientproteins |
| spellingShingle |
Assisted protein folding at low temperature: evolutionaryadaptation of the Antarctic fish chaperonin CCT and its clientproteins Cuellar, Jorge CCT TriC Chaperone Chaperonin Protein folding Actin Tubulin Thermal adaptation Evolution |
| title_short |
Assisted protein folding at low temperature: evolutionaryadaptation of the Antarctic fish chaperonin CCT and its clientproteins |
| title_full |
Assisted protein folding at low temperature: evolutionaryadaptation of the Antarctic fish chaperonin CCT and its clientproteins |
| title_fullStr |
Assisted protein folding at low temperature: evolutionaryadaptation of the Antarctic fish chaperonin CCT and its clientproteins |
| title_full_unstemmed |
Assisted protein folding at low temperature: evolutionaryadaptation of the Antarctic fish chaperonin CCT and its clientproteins |
| title_sort |
Assisted protein folding at low temperature: evolutionaryadaptation of the Antarctic fish chaperonin CCT and its clientproteins |
| dc.creator.none.fl_str_mv |
Cuellar, Jorge Yébenes, Hugo Parker, Sandra K. Carranza Ferrer, Gerardo|||0000-0003-1081-7850 Serna, Marina Valpuesta Moralejo, José María Zabala Otaño, Juan Carlos|||0000-0003-2679-5473 Detrich, H. William |
| author |
Cuellar, Jorge |
| author_facet |
Cuellar, Jorge Yébenes, Hugo Parker, Sandra K. Carranza Ferrer, Gerardo|||0000-0003-1081-7850 Serna, Marina Valpuesta Moralejo, José María Zabala Otaño, Juan Carlos|||0000-0003-2679-5473 Detrich, H. William |
| author_role |
author |
| author2 |
Yébenes, Hugo Parker, Sandra K. Carranza Ferrer, Gerardo|||0000-0003-1081-7850 Serna, Marina Valpuesta Moralejo, José María Zabala Otaño, Juan Carlos|||0000-0003-2679-5473 Detrich, H. William |
| author2_role |
author author author author author author author |
| dc.contributor.none.fl_str_mv |
Universidad de Cantabria |
| dc.subject.none.fl_str_mv |
CCT TriC Chaperone Chaperonin Protein folding Actin Tubulin Thermal adaptation Evolution |
| topic |
CCT TriC Chaperone Chaperonin Protein folding Actin Tubulin Thermal adaptation Evolution |
| description |
Eukaryotic ectotherms of the Southern Ocean face energetic challenges to protein folding assisted by the cytosolic chaperonin CCT. We hypothesize that CCT and its client proteins (CPs) have co-evolved molecular adaptations that facilitate CCT–CP interaction and the ATP-driven folding cycle at low temperature. To test this hypothesis, we compared the functional and structural properties of CCT–CP systems from testis tissues of an Antarctic fish, Gobionotothen gibberifrons (Lo¨nnberg) (habitat/body T=-1.9 to +2˚C), and of the cow (body T=37˚C). We examined the temperature dependence of the binding of denatured CPs (bactin, b-tubulin) by fish and bovine CCTs, both in homologous and heterologous combinations and at temperatures between 24˚C and 20˚C, in a buffer conducive to binding of the denatured CP to the open conformation of CCT. In homologous combination, the percentage of G. gibberifrons CCT bound to CP declined linearly with increasing temperature, whereas the converse was true for bovine CCT. Binding of CCT to heterologous CPs was low, irrespective of temperature. When reactions were supplemented with ATP, G. gibberifrons CCT catalyzed the folding and release of actin at 2˚C. The ATPase activity of apo-CCT from G. gibberifrons at 4˚C was, 2.5-fold greater than that of apo-bovine CCT, whereas equivalent activities were observed at 20˚C. Based on these results, we conclude that the catalytic folding cycle of CCT from Antarctic fishes is partially compensated at their habitat temperature, probably by means of enhanced CP-binding affinity and increased flexibility of the CCT subunits. |
| publishDate |
2014 |
| dc.date.none.fl_str_mv |
2014 2014-04-15 |
| dc.type.none.fl_str_mv |
journal article http://purl.org/coar/resource_type/c_6501 NA http://purl.org/coar/version/c_be7fb7dd8ff6fe43 |
| dc.type.openaire.fl_str_mv |
info:eu-repo/semantics/article |
| format |
article |
| dc.identifier.none.fl_str_mv |
http://hdl.handle.net/10902/7814 |
| url |
http://hdl.handle.net/10902/7814 |
| dc.language.none.fl_str_mv |
Inglés eng |
| language_invalid_str_mv |
Inglés |
| language |
eng |
| dc.rights.none.fl_str_mv |
open access http://purl.org/coar/access_right/c_abf2 Atribución 3.0 España http://creativecommons.org/licenses/by/3.0/es/ |
| dc.rights.openaire.fl_str_mv |
info:eu-repo/semantics/openAccess |
| rights_invalid_str_mv |
open access http://purl.org/coar/access_right/c_abf2 Atribución 3.0 España http://creativecommons.org/licenses/by/3.0/es/ |
| eu_rights_str_mv |
openAccess |
| dc.publisher.none.fl_str_mv |
The Company of Biologists Ltd |
| publisher.none.fl_str_mv |
The Company of Biologists Ltd |
| dc.source.none.fl_str_mv |
Biology Open 2014 Apr 15; 3(4): 261–270 reponame:UCrea Repositorio Abierto de la Universidad de Cantabria instname:Universidad de Cantabria (UC) |
| instname_str |
Universidad de Cantabria (UC) |
| reponame_str |
UCrea Repositorio Abierto de la Universidad de Cantabria |
| collection |
UCrea Repositorio Abierto de la Universidad de Cantabria |
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|
| repository.mail.fl_str_mv |
|
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1869406201535528960 |
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15.301603 |