A proteomic approach toward the selection of proteins with enhanced intrinsic conformational stability

Detalhes bibliográficos
Autor(a) principal: Prosinecki, Vesna
Data de Publicação: 2006
Outros Autores: Botelho, Hugo M., Francese, Simona, Mastrobuoni, Guido, Moneti, Gloriano, Urich, Tim, Kletzin, Arnulf, Gomes, Cláudio M.
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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spelling 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)
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