Metal ions modulate the folding and stability of the tumor suppressor protein S100A2

Detalhes bibliográficos
Autor(a) principal: Botelho, Hugo M.
Data de Publicação: 2009
Outros Autores: Koch, Michael, Fritz, Günter, 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/10362/5452
Resumo: Febs Journal (2009)276:1776-1786
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spelling Metal ions modulate the folding and stability of the tumor suppressor protein S100A2cancermetalsp53protein stabilityprotein structure and foldingFebs Journal (2009)276:1776-1786The EF-hand protein S100A2 is a cell cycle regulator involved in tumorigenesis, acting through regulation of the p53 activation state. Metal ion-free S100A2 is homodimeric and contains two Ca2+-binding sites and two Zn2+-binding sites per subunit, whereby the Zn2+ ion binding to one of the sites is coordinated by residues from two homodimers. The effect of selective binding of these metal ions was investigated using site-specific mutants which lacked one or both zinc sites. CD analysis of secondary structure changes on metallation showed that Zn2+ binding was associated with a decrease in the secondary structure content, whereas Ca2+ had the opposite effect in two of the three S100A2 mutants studied. The energy of unfolding DeltaGU of the apo wild-type S100A2 was determined to be 89.9 kJ.mol-1, and the apparent midpoint transition temperature (Tmapp) was 58.4ºC. In addition, a detailed study of the urea and thermal unfolding of the S100A2 mutants in different metallation states (apo, Zn2+ and Ca2+) was performed. Thermal denaturation experiments showed that Zn2+ acts as a destabilizer and Ca2+ as a stabilizer of the protein conformation. This suggests a synergistic effect between metal binding, protein stability and S100A2 biological activity, according to which Ca2+ activates and stabilizes the protein, the opposite being observed on Zn2+ binding.WileyRUNBotelho, Hugo M.Koch, MichaelFritz, GünterGomes, Cláudio M.2011-04-05T15:22:22Z2009-03-102009-03-10T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfapplication/pdfhttp://hdl.handle.net/10362/5452engBotelho, H. M., Koch, M., Fritz, G., and Gomes, C. M. (2009) Metal ions modulate the folding and stability of the tumor suppressor protein S100A2, Febs J 276, 1776-1786metadata only accessinfo: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:10362/5452Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:16:16.859944Repositório 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 Metal ions modulate the folding and stability of the tumor suppressor protein S100A2
title Metal ions modulate the folding and stability of the tumor suppressor protein S100A2
spellingShingle Metal ions modulate the folding and stability of the tumor suppressor protein S100A2
Botelho, Hugo M.
cancer
metals
p53
protein stability
protein structure and folding
title_short Metal ions modulate the folding and stability of the tumor suppressor protein S100A2
title_full Metal ions modulate the folding and stability of the tumor suppressor protein S100A2
title_fullStr Metal ions modulate the folding and stability of the tumor suppressor protein S100A2
title_full_unstemmed Metal ions modulate the folding and stability of the tumor suppressor protein S100A2
title_sort Metal ions modulate the folding and stability of the tumor suppressor protein S100A2
author Botelho, Hugo M.
author_facet Botelho, Hugo M.
Koch, Michael
Fritz, Günter
Gomes, Cláudio M.
author_role author
author2 Koch, Michael
Fritz, Günter
Gomes, Cláudio M.
author2_role author
author
author
dc.contributor.none.fl_str_mv RUN
dc.contributor.author.fl_str_mv Botelho, Hugo M.
Koch, Michael
Fritz, Günter
Gomes, Cláudio M.
dc.subject.por.fl_str_mv cancer
metals
p53
protein stability
protein structure and folding
topic cancer
metals
p53
protein stability
protein structure and folding
description Febs Journal (2009)276:1776-1786
publishDate 2009
dc.date.none.fl_str_mv 2009-03-10
2009-03-10T00:00:00Z
2011-04-05T15:22:22Z
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/10362/5452
url http://hdl.handle.net/10362/5452
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Botelho, H. M., Koch, M., Fritz, G., and Gomes, C. M. (2009) Metal ions modulate the folding and stability of the tumor suppressor protein S100A2, Febs J 276, 1776-1786
dc.rights.driver.fl_str_mv metadata only access
info:eu-repo/semantics/openAccess
rights_invalid_str_mv metadata only access
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Wiley
publisher.none.fl_str_mv Wiley
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
instacron_str RCAAP
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collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
repository.mail.fl_str_mv
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