CGDEase, a Pseudomonas fluorescens protein of the PLC/APase superfamily with CDP-ethanolamine and (dihexanoyl) glycerophosphoethanolamine hydrolase activity induced by osmoprotectants under phosphate-deficient conditions
Autor(a) principal: | |
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Data de Publicação: | 2010 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | por |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10174/5780 |
Resumo: | A novel enzyme, induced by choline, ethanolamine, glycine betaine or dimethylglycine, was released at low temperature and phosphate from Pseudomonas fluorescens (CECT 7229) suspensions at low cell densities. It is a CDP-ethanolamine pyrophosphatase/(dihexanoyl)glycerophosphoethanolamine phosphodiesterase (CGDEase) less active on choline derivatives, and inactive on long-chain phospholipids, CDP-glycerol and other NDP-X compounds. The reaction pattern was typical of phospholipase C (PLC), as either phosphoethanolamine or phosphocholine was produced. Peptide-mass analyses, gene cloning and expression provided a molecular identity for CGDEase. Bioinformatic studies assigned it to the PLC branch of the phospholipase C/acid phosphatase (PLC/APase) superfamily, revealed an irregular phylogenetic distribution of close CGDEase relatives, and suggested their genes are not in operons or conserved contexts. A theoretical CGDEase structure was supported by mutagenesis of two predicted active-site residues, which yielded essentially inactive mutants. Biological relevance is supported by comparisons with CGDEase relatives, induction by osmoprotectants (not by osmotic stress itself) and repression by micromolar phosphate. The low bacterial density requirement was related to phosphate liberation from lysed bacteria in denser populations, rather than to a classical quorum-sensing effect. The results fit better a CGDEase role in phosphate scavenging than in osmoprotection. |
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CGDEase, a Pseudomonas fluorescens protein of the PLC/APase superfamily with CDP-ethanolamine and (dihexanoyl) glycerophosphoethanolamine hydrolase activity induced by osmoprotectants under phosphate-deficient conditionsPseudomonas fluorescensCDP-ethanolamine pyrophosphatase/ (dihexanoyl)glycerophosphoethanolamine phosphodiesterasePLC/APaseA novel enzyme, induced by choline, ethanolamine, glycine betaine or dimethylglycine, was released at low temperature and phosphate from Pseudomonas fluorescens (CECT 7229) suspensions at low cell densities. It is a CDP-ethanolamine pyrophosphatase/(dihexanoyl)glycerophosphoethanolamine phosphodiesterase (CGDEase) less active on choline derivatives, and inactive on long-chain phospholipids, CDP-glycerol and other NDP-X compounds. The reaction pattern was typical of phospholipase C (PLC), as either phosphoethanolamine or phosphocholine was produced. Peptide-mass analyses, gene cloning and expression provided a molecular identity for CGDEase. Bioinformatic studies assigned it to the PLC branch of the phospholipase C/acid phosphatase (PLC/APase) superfamily, revealed an irregular phylogenetic distribution of close CGDEase relatives, and suggested their genes are not in operons or conserved contexts. A theoretical CGDEase structure was supported by mutagenesis of two predicted active-site residues, which yielded essentially inactive mutants. Biological relevance is supported by comparisons with CGDEase relatives, induction by osmoprotectants (not by osmotic stress itself) and repression by micromolar phosphate. The low bacterial density requirement was related to phosphate liberation from lysed bacteria in denser populations, rather than to a classical quorum-sensing effect. The results fit better a CGDEase role in phosphate scavenging than in osmoprotection.2012-11-20T11:48:05Z2012-11-202010-10-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://hdl.handle.net/10174/5780http://hdl.handle.net/10174/5780porCostas MJ, Pinto RM, Cordero PM, Cabezas A, Alves-Pereira I, Cameselle C, Ribeiro JM (2010) CGDEase, a Pseudomonas fluorescens protein of the PLC/APase superfamily with CDP-ethanolamine and (dihexanoyl) glycerophosphoethanolamine hydrolase activity induced by osmoprotectants under phosphate-deficient conditions. Molecular microbiology, 78:1556-1576. doi: 10.1111/j.1365-2958.2010.07425.xhttp://onlinelibrary.wiley.com/doi/10.1111/j.1365-2958.2010.07425.x/abstractICAAMndndndiap@uevora.ptndnd365Costas, MJCordero, PMCabezas, AAlves-Pereira, ICameselle, CRibeiro, JMinfo: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:RCAAP2024-01-03T18:44:16Zoai:dspace.uevora.pt:10174/5780Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T01:00:29.951878Repositório 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 |
CGDEase, a Pseudomonas fluorescens protein of the PLC/APase superfamily with CDP-ethanolamine and (dihexanoyl) glycerophosphoethanolamine hydrolase activity induced by osmoprotectants under phosphate-deficient conditions |
title |
CGDEase, a Pseudomonas fluorescens protein of the PLC/APase superfamily with CDP-ethanolamine and (dihexanoyl) glycerophosphoethanolamine hydrolase activity induced by osmoprotectants under phosphate-deficient conditions |
spellingShingle |
CGDEase, a Pseudomonas fluorescens protein of the PLC/APase superfamily with CDP-ethanolamine and (dihexanoyl) glycerophosphoethanolamine hydrolase activity induced by osmoprotectants under phosphate-deficient conditions Costas, MJ Pseudomonas fluorescens CDP-ethanolamine pyrophosphatase/ (dihexanoyl)glycerophosphoethanolamine phosphodiesterase PLC/APase |
title_short |
CGDEase, a Pseudomonas fluorescens protein of the PLC/APase superfamily with CDP-ethanolamine and (dihexanoyl) glycerophosphoethanolamine hydrolase activity induced by osmoprotectants under phosphate-deficient conditions |
title_full |
CGDEase, a Pseudomonas fluorescens protein of the PLC/APase superfamily with CDP-ethanolamine and (dihexanoyl) glycerophosphoethanolamine hydrolase activity induced by osmoprotectants under phosphate-deficient conditions |
title_fullStr |
CGDEase, a Pseudomonas fluorescens protein of the PLC/APase superfamily with CDP-ethanolamine and (dihexanoyl) glycerophosphoethanolamine hydrolase activity induced by osmoprotectants under phosphate-deficient conditions |
title_full_unstemmed |
CGDEase, a Pseudomonas fluorescens protein of the PLC/APase superfamily with CDP-ethanolamine and (dihexanoyl) glycerophosphoethanolamine hydrolase activity induced by osmoprotectants under phosphate-deficient conditions |
title_sort |
CGDEase, a Pseudomonas fluorescens protein of the PLC/APase superfamily with CDP-ethanolamine and (dihexanoyl) glycerophosphoethanolamine hydrolase activity induced by osmoprotectants under phosphate-deficient conditions |
author |
Costas, MJ |
author_facet |
Costas, MJ Cordero, PM Cabezas, A Alves-Pereira, I Cameselle, C Ribeiro, JM |
author_role |
author |
author2 |
Cordero, PM Cabezas, A Alves-Pereira, I Cameselle, C Ribeiro, JM |
author2_role |
author author author author author |
dc.contributor.author.fl_str_mv |
Costas, MJ Cordero, PM Cabezas, A Alves-Pereira, I Cameselle, C Ribeiro, JM |
dc.subject.por.fl_str_mv |
Pseudomonas fluorescens CDP-ethanolamine pyrophosphatase/ (dihexanoyl)glycerophosphoethanolamine phosphodiesterase PLC/APase |
topic |
Pseudomonas fluorescens CDP-ethanolamine pyrophosphatase/ (dihexanoyl)glycerophosphoethanolamine phosphodiesterase PLC/APase |
description |
A novel enzyme, induced by choline, ethanolamine, glycine betaine or dimethylglycine, was released at low temperature and phosphate from Pseudomonas fluorescens (CECT 7229) suspensions at low cell densities. It is a CDP-ethanolamine pyrophosphatase/(dihexanoyl)glycerophosphoethanolamine phosphodiesterase (CGDEase) less active on choline derivatives, and inactive on long-chain phospholipids, CDP-glycerol and other NDP-X compounds. The reaction pattern was typical of phospholipase C (PLC), as either phosphoethanolamine or phosphocholine was produced. Peptide-mass analyses, gene cloning and expression provided a molecular identity for CGDEase. Bioinformatic studies assigned it to the PLC branch of the phospholipase C/acid phosphatase (PLC/APase) superfamily, revealed an irregular phylogenetic distribution of close CGDEase relatives, and suggested their genes are not in operons or conserved contexts. A theoretical CGDEase structure was supported by mutagenesis of two predicted active-site residues, which yielded essentially inactive mutants. Biological relevance is supported by comparisons with CGDEase relatives, induction by osmoprotectants (not by osmotic stress itself) and repression by micromolar phosphate. The low bacterial density requirement was related to phosphate liberation from lysed bacteria in denser populations, rather than to a classical quorum-sensing effect. The results fit better a CGDEase role in phosphate scavenging than in osmoprotection. |
publishDate |
2010 |
dc.date.none.fl_str_mv |
2010-10-01T00:00:00Z 2012-11-20T11:48:05Z 2012-11-20 |
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/10174/5780 http://hdl.handle.net/10174/5780 |
url |
http://hdl.handle.net/10174/5780 |
dc.language.iso.fl_str_mv |
por |
language |
por |
dc.relation.none.fl_str_mv |
Costas MJ, Pinto RM, Cordero PM, Cabezas A, Alves-Pereira I, Cameselle C, Ribeiro JM (2010) CGDEase, a Pseudomonas fluorescens protein of the PLC/APase superfamily with CDP-ethanolamine and (dihexanoyl) glycerophosphoethanolamine hydrolase activity induced by osmoprotectants under phosphate-deficient conditions. Molecular microbiology, 78:1556-1576. doi: 10.1111/j.1365-2958.2010.07425.x http://onlinelibrary.wiley.com/doi/10.1111/j.1365-2958.2010.07425.x/abstract ICAAM nd nd nd iap@uevora.pt nd nd 365 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
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 |
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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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