A proteomic approach toward the selection of proteins with enhanced intrinsic conformational stability
Autor(a) principal: | |
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Data de Publicação: | 2006 |
Outros Autores: | , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10362/5451 |
Resumo: | Journal of Proteome Research (2006)5: 2720-2726 |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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7160 |
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A proteomic approach toward the selection of proteins with enhanced intrinsic conformational stabilityArchaeaThermophilesProtein Folding and StabilitySuperoxide dismutaseFerredoxinJournal of Proteome Research (2006)5: 2720-2726A detailed understanding of the molecular basis of protein folding and stability determinants partly relies on the study of proteins with enhanced conformational stability properties, such as those from thermophilic organisms. In this study we set up a methodology aiming at identifying the subset of cytosolic hyperstable proteins using Sulfurispharea sp., a hyperthermophilic archaeon, able to grow between 70-97°C, as a model organism. We have thermally and chemically perturbed the cytosolic proteome as a function of time (up to 96h incubation at 90°C), and proceeded with analysis of the remaining proteins by combining one and two dimensional gel electrophoresis, liquid chromatography fractionation, and protein identification by N-terminal sequencing and mass spectrometry methods. A total of 14 proteins with enhanced stabilities which are involved in key cellular processes such as detoxification, nucleic acid processing and energy metabolism were identified including a superoxide dismutase, a peroxiredoxin and a ferredoxin. We demonstrate that these proteins are biologically active after extensive thermal treatment of the proteome. The relevance of these and other targets is discussed in terms of the organism’s ecology. This work thus illustrates an experimental approach aimed at mining a proteome for hyperstable proteins, a valuable tool for target selection in protein stability and structural studies.American Chemical SocietyRUNProsinecki, VesnaBotelho, Hugo M.Francese, SimonaMastrobuoni, GuidoMoneti, GlorianoUrich, TimKletzin, ArnulfGomes, Cláudio M.2011-04-05T15:22:06Z2006-08-262006-08-26T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfapplication/pdfhttp://hdl.handle.net/10362/5451engProsinecki, V., Botelho, H. M., Francese, S., Mastrobuoni, G., Moneti, G., Urich, T., Kletzin, A., and Gomes, C. M. (2006) A proteomic approach toward the selection of proteins with enhanced intrinsic conformational stability, J Proteome Res 5, 2720-2726info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-03-11T03:35:59Zoai:run.unl.pt:10362/5451Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:16:16.681689Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
A proteomic approach toward the selection of proteins with enhanced intrinsic conformational stability |
title |
A proteomic approach toward the selection of proteins with enhanced intrinsic conformational stability |
spellingShingle |
A proteomic approach toward the selection of proteins with enhanced intrinsic conformational stability Prosinecki, Vesna Archaea Thermophiles Protein Folding and Stability Superoxide dismutase Ferredoxin |
title_short |
A proteomic approach toward the selection of proteins with enhanced intrinsic conformational stability |
title_full |
A proteomic approach toward the selection of proteins with enhanced intrinsic conformational stability |
title_fullStr |
A proteomic approach toward the selection of proteins with enhanced intrinsic conformational stability |
title_full_unstemmed |
A proteomic approach toward the selection of proteins with enhanced intrinsic conformational stability |
title_sort |
A proteomic approach toward the selection of proteins with enhanced intrinsic conformational stability |
author |
Prosinecki, Vesna |
author_facet |
Prosinecki, Vesna Botelho, Hugo M. Francese, Simona Mastrobuoni, Guido Moneti, Gloriano Urich, Tim Kletzin, Arnulf Gomes, Cláudio M. |
author_role |
author |
author2 |
Botelho, Hugo M. Francese, Simona Mastrobuoni, Guido Moneti, Gloriano Urich, Tim Kletzin, Arnulf Gomes, Cláudio M. |
author2_role |
author author author author author author author |
dc.contributor.none.fl_str_mv |
RUN |
dc.contributor.author.fl_str_mv |
Prosinecki, Vesna Botelho, Hugo M. Francese, Simona Mastrobuoni, Guido Moneti, Gloriano Urich, Tim Kletzin, Arnulf Gomes, Cláudio M. |
dc.subject.por.fl_str_mv |
Archaea Thermophiles Protein Folding and Stability Superoxide dismutase Ferredoxin |
topic |
Archaea Thermophiles Protein Folding and Stability Superoxide dismutase Ferredoxin |
description |
Journal of Proteome Research (2006)5: 2720-2726 |
publishDate |
2006 |
dc.date.none.fl_str_mv |
2006-08-26 2006-08-26T00:00:00Z 2011-04-05T15:22:06Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10362/5451 |
url |
http://hdl.handle.net/10362/5451 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Prosinecki, V., Botelho, H. M., Francese, S., Mastrobuoni, G., Moneti, G., Urich, T., Kletzin, A., and Gomes, C. M. (2006) A proteomic approach toward the selection of proteins with enhanced intrinsic conformational stability, J Proteome Res 5, 2720-2726 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
American Chemical Society |
publisher.none.fl_str_mv |
American Chemical Society |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
instname_str |
Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
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RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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|
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1799137812807680000 |