Desulfovibrio gigas neelaredoxin: a novel superoxide dismutase integrated in a putative oxygen sensory operon of an anaerobe
Autor(a) principal: | |
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Data de Publicação: | 1999 |
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/10174/2110 |
Resumo: | Neelaredoxin, a small non-heme blue iron protein from the sulfate-reducing bacterium Desulfovibrio gigas [Chen, L., Sharma, P., LeGall, J., Mariano, A.M., Teixeira M. and Xavier, A.V. (1994) Eur. J. Biochem. 226, 613±618] is shown to be encoded by a polycistronic unit which contains two additional open reading frames (ORF-1 and ORF-2) coding for chemotaxis-like proteins. ORF-1 has domains highly homologous with those structurally and functionally important in methyl-accepting chemotaxis proteins, including two putative transmembrane helices, potential methylation sites and the interaction domain with CheW proteins. Interestingly, ORF-2 encodes a protein having homologies with CheW proteins. Neelaredoxin is also shown to have significant superoxide dismutase activity (1200 U´mg±1), making it a novel type of iron superoxide dismutase. Analysis of genomic data shows that neelaredoxin-like putative polypeptides are present in strict anaerobic archaea, suggesting that this is a primordial superoxide dismutase. The three proteins encoded in this operon may be involved in the oxygen-sensing mechanisms of this anaerobic bacterium, indicating a possible transcriptional mechanism to sense and respond to potential stress agents. |
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Desulfovibrio gigas neelaredoxin: a novel superoxide dismutase integrated in a putative oxygen sensory operon of an anaerobeDesulfovibrio gigasneelaredoxinNeelaredoxin, a small non-heme blue iron protein from the sulfate-reducing bacterium Desulfovibrio gigas [Chen, L., Sharma, P., LeGall, J., Mariano, A.M., Teixeira M. and Xavier, A.V. (1994) Eur. J. Biochem. 226, 613±618] is shown to be encoded by a polycistronic unit which contains two additional open reading frames (ORF-1 and ORF-2) coding for chemotaxis-like proteins. ORF-1 has domains highly homologous with those structurally and functionally important in methyl-accepting chemotaxis proteins, including two putative transmembrane helices, potential methylation sites and the interaction domain with CheW proteins. Interestingly, ORF-2 encodes a protein having homologies with CheW proteins. Neelaredoxin is also shown to have significant superoxide dismutase activity (1200 U´mg±1), making it a novel type of iron superoxide dismutase. Analysis of genomic data shows that neelaredoxin-like putative polypeptides are present in strict anaerobic archaea, suggesting that this is a primordial superoxide dismutase. The three proteins encoded in this operon may be involved in the oxygen-sensing mechanisms of this anaerobic bacterium, indicating a possible transcriptional mechanism to sense and respond to potential stress agents.2010-09-28T10:36:18Z2010-09-281999-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article30874 bytesapplication/pdfhttp://hdl.handle.net/10174/2110http://hdl.handle.net/10174/2110engpag 235-243259European Journal of Biochemistry259livrendndndndndndndndnd552Silva, GabrielaOliveira, SolangeGomes, CláudioPacheco, IsabelLiu, M.Y.Xavier, António V.Teixeira, MiguelLeGall, JeanRodrigues-Pousada, Claudinainfo: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:RCAAP2024-01-03T18:38:17Zoai:dspace.uevora.pt:10174/2110Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T00:57:52.702468Repositório 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 |
Desulfovibrio gigas neelaredoxin: a novel superoxide dismutase integrated in a putative oxygen sensory operon of an anaerobe |
title |
Desulfovibrio gigas neelaredoxin: a novel superoxide dismutase integrated in a putative oxygen sensory operon of an anaerobe |
spellingShingle |
Desulfovibrio gigas neelaredoxin: a novel superoxide dismutase integrated in a putative oxygen sensory operon of an anaerobe Silva, Gabriela Desulfovibrio gigas neelaredoxin |
title_short |
Desulfovibrio gigas neelaredoxin: a novel superoxide dismutase integrated in a putative oxygen sensory operon of an anaerobe |
title_full |
Desulfovibrio gigas neelaredoxin: a novel superoxide dismutase integrated in a putative oxygen sensory operon of an anaerobe |
title_fullStr |
Desulfovibrio gigas neelaredoxin: a novel superoxide dismutase integrated in a putative oxygen sensory operon of an anaerobe |
title_full_unstemmed |
Desulfovibrio gigas neelaredoxin: a novel superoxide dismutase integrated in a putative oxygen sensory operon of an anaerobe |
title_sort |
Desulfovibrio gigas neelaredoxin: a novel superoxide dismutase integrated in a putative oxygen sensory operon of an anaerobe |
author |
Silva, Gabriela |
author_facet |
Silva, Gabriela Oliveira, Solange Gomes, Cláudio Pacheco, Isabel Liu, M.Y. Xavier, António V. Teixeira, Miguel LeGall, Jean Rodrigues-Pousada, Claudina |
author_role |
author |
author2 |
Oliveira, Solange Gomes, Cláudio Pacheco, Isabel Liu, M.Y. Xavier, António V. Teixeira, Miguel LeGall, Jean Rodrigues-Pousada, Claudina |
author2_role |
author author author author author author author author |
dc.contributor.author.fl_str_mv |
Silva, Gabriela Oliveira, Solange Gomes, Cláudio Pacheco, Isabel Liu, M.Y. Xavier, António V. Teixeira, Miguel LeGall, Jean Rodrigues-Pousada, Claudina |
dc.subject.por.fl_str_mv |
Desulfovibrio gigas neelaredoxin |
topic |
Desulfovibrio gigas neelaredoxin |
description |
Neelaredoxin, a small non-heme blue iron protein from the sulfate-reducing bacterium Desulfovibrio gigas [Chen, L., Sharma, P., LeGall, J., Mariano, A.M., Teixeira M. and Xavier, A.V. (1994) Eur. J. Biochem. 226, 613±618] is shown to be encoded by a polycistronic unit which contains two additional open reading frames (ORF-1 and ORF-2) coding for chemotaxis-like proteins. ORF-1 has domains highly homologous with those structurally and functionally important in methyl-accepting chemotaxis proteins, including two putative transmembrane helices, potential methylation sites and the interaction domain with CheW proteins. Interestingly, ORF-2 encodes a protein having homologies with CheW proteins. Neelaredoxin is also shown to have significant superoxide dismutase activity (1200 U´mg±1), making it a novel type of iron superoxide dismutase. Analysis of genomic data shows that neelaredoxin-like putative polypeptides are present in strict anaerobic archaea, suggesting that this is a primordial superoxide dismutase. The three proteins encoded in this operon may be involved in the oxygen-sensing mechanisms of this anaerobic bacterium, indicating a possible transcriptional mechanism to sense and respond to potential stress agents. |
publishDate |
1999 |
dc.date.none.fl_str_mv |
1999-01-01T00:00:00Z 2010-09-28T10:36:18Z 2010-09-28 |
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/10174/2110 http://hdl.handle.net/10174/2110 |
url |
http://hdl.handle.net/10174/2110 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
pag 235-243 259 European Journal of Biochemistry 259 livre nd nd nd nd nd nd nd nd nd 552 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
30874 bytes application/pdf |
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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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