Metal ions modulate the folding and stability of the tumor suppressor protein S100A2
Autor(a) principal: | |
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Data de Publicação: | 2009 |
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/10362/5452 |
Resumo: | Febs Journal (2009)276:1776-1786 |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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7160 |
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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 |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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 |
|
_version_ |
1799137812811874304 |