Saccharomyces cerevisiae Hog1 protein phosphorylation upon exposure to bacterial endotoxin
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/10316/12631 https://doi.org/10.1074/jbc.M603753200 |
Resumo: | The yeast Hog1 protein is both functionally and structurally similar to the mammalian p38, belonging to the same family of mitogen-activated protein (MAP) kinases and responding to extracellular changes in osmolarity. Since p38 mediates lipopolysaccharide (LPS) effects in mammalian cells, we now tested the responsiveness of Hog1 upon exposure of the yeast Saccharomyces cerevisiae to bacterial LPS. In the presence of Escherichia coli LPS (100 ng/ml) and an endotoxically active, hexaacylated, synthetic lipid A (compound 506; 100 ng/ml), Hog1 becomes phosphorylated with a maximum of phosphorylation between 3 and 6 h, whereas a tetraacylated, inactive form of lipid A (compound 406) did not cause any modification in the phosphorylation state of Hog1. A triple labeling immunocytochemical study showed that phosphorylated Hog1 translocates into the nucleus after a 90-min incubation and becomes sparsely located in the cytoplasm. The translocation of the phospho-Hog1 is preceded by an increased expression of the HOG1 gene and concomitant with the expression of the Hog1 target gene, GPD1. We also observed that cells unable to synthesize Hog1 do not resist LPS as efficiently as wild-type cells. We conclude that the yeast S. cerevisiae is able to respond to the presence of Gram-negative bacteria endotoxin and that Hog1 is involved in this response |
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Saccharomyces cerevisiae Hog1 protein phosphorylation upon exposure to bacterial endotoxinThe yeast Hog1 protein is both functionally and structurally similar to the mammalian p38, belonging to the same family of mitogen-activated protein (MAP) kinases and responding to extracellular changes in osmolarity. Since p38 mediates lipopolysaccharide (LPS) effects in mammalian cells, we now tested the responsiveness of Hog1 upon exposure of the yeast Saccharomyces cerevisiae to bacterial LPS. In the presence of Escherichia coli LPS (100 ng/ml) and an endotoxically active, hexaacylated, synthetic lipid A (compound 506; 100 ng/ml), Hog1 becomes phosphorylated with a maximum of phosphorylation between 3 and 6 h, whereas a tetraacylated, inactive form of lipid A (compound 406) did not cause any modification in the phosphorylation state of Hog1. A triple labeling immunocytochemical study showed that phosphorylated Hog1 translocates into the nucleus after a 90-min incubation and becomes sparsely located in the cytoplasm. The translocation of the phospho-Hog1 is preceded by an increased expression of the HOG1 gene and concomitant with the expression of the Hog1 target gene, GPD1. We also observed that cells unable to synthesize Hog1 do not resist LPS as efficiently as wild-type cells. We conclude that the yeast S. cerevisiae is able to respond to the presence of Gram-negative bacteria endotoxin and that Hog1 is involved in this responseThe American Society for Biochemistry and Molecular Biology2006-08-25info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://hdl.handle.net/10316/12631http://hdl.handle.net/10316/12631https://doi.org/10.1074/jbc.M603753200engThe Journal of Biological Chemistry. 281:34 (2006) 24687-246940021-9258Marques, Joana M.Rodrigues, Ricardo J.Sant'Ana, Augusto C. de MagalhãesGonçalves, Teresainfo: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:RCAAP2022-05-25T03:59:36Zoai:estudogeral.uc.pt:10316/12631Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T20:43:37.441371Repositório 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 |
Saccharomyces cerevisiae Hog1 protein phosphorylation upon exposure to bacterial endotoxin |
title |
Saccharomyces cerevisiae Hog1 protein phosphorylation upon exposure to bacterial endotoxin |
spellingShingle |
Saccharomyces cerevisiae Hog1 protein phosphorylation upon exposure to bacterial endotoxin Marques, Joana M. |
title_short |
Saccharomyces cerevisiae Hog1 protein phosphorylation upon exposure to bacterial endotoxin |
title_full |
Saccharomyces cerevisiae Hog1 protein phosphorylation upon exposure to bacterial endotoxin |
title_fullStr |
Saccharomyces cerevisiae Hog1 protein phosphorylation upon exposure to bacterial endotoxin |
title_full_unstemmed |
Saccharomyces cerevisiae Hog1 protein phosphorylation upon exposure to bacterial endotoxin |
title_sort |
Saccharomyces cerevisiae Hog1 protein phosphorylation upon exposure to bacterial endotoxin |
author |
Marques, Joana M. |
author_facet |
Marques, Joana M. Rodrigues, Ricardo J. Sant'Ana, Augusto C. de Magalhães Gonçalves, Teresa |
author_role |
author |
author2 |
Rodrigues, Ricardo J. Sant'Ana, Augusto C. de Magalhães Gonçalves, Teresa |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
Marques, Joana M. Rodrigues, Ricardo J. Sant'Ana, Augusto C. de Magalhães Gonçalves, Teresa |
description |
The yeast Hog1 protein is both functionally and structurally similar to the mammalian p38, belonging to the same family of mitogen-activated protein (MAP) kinases and responding to extracellular changes in osmolarity. Since p38 mediates lipopolysaccharide (LPS) effects in mammalian cells, we now tested the responsiveness of Hog1 upon exposure of the yeast Saccharomyces cerevisiae to bacterial LPS. In the presence of Escherichia coli LPS (100 ng/ml) and an endotoxically active, hexaacylated, synthetic lipid A (compound 506; 100 ng/ml), Hog1 becomes phosphorylated with a maximum of phosphorylation between 3 and 6 h, whereas a tetraacylated, inactive form of lipid A (compound 406) did not cause any modification in the phosphorylation state of Hog1. A triple labeling immunocytochemical study showed that phosphorylated Hog1 translocates into the nucleus after a 90-min incubation and becomes sparsely located in the cytoplasm. The translocation of the phospho-Hog1 is preceded by an increased expression of the HOG1 gene and concomitant with the expression of the Hog1 target gene, GPD1. We also observed that cells unable to synthesize Hog1 do not resist LPS as efficiently as wild-type cells. We conclude that the yeast S. cerevisiae is able to respond to the presence of Gram-negative bacteria endotoxin and that Hog1 is involved in this response |
publishDate |
2006 |
dc.date.none.fl_str_mv |
2006-08-25 |
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/10316/12631 http://hdl.handle.net/10316/12631 https://doi.org/10.1074/jbc.M603753200 |
url |
http://hdl.handle.net/10316/12631 https://doi.org/10.1074/jbc.M603753200 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
The Journal of Biological Chemistry. 281:34 (2006) 24687-24694 0021-9258 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.publisher.none.fl_str_mv |
The American Society for Biochemistry and Molecular Biology |
publisher.none.fl_str_mv |
The American Society for Biochemistry and Molecular Biology |
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) |
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 |
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1799133707928338432 |