Impaired polyhydroxybutyrate biosynthesis from glucose in Pseudomonas sp. 14-3 is due to a defective β-ketothiolase gene
- Autores
- Ayub, N.D.; Julia Pettinari, M.; Méndez, B.S.; López, N.I.
- Año de publicación
- 2006
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Pseudomonas sp. 14-3 accumulates polyhydroxybutyrate (PHB) from octanoate, but not from glucose. To elucidate this unusual phenotype, genes responsible for the synthesis of PHB were cloned and analyzed. A PHB polymerase gene (phaC) was found downstream from genes coding for a β-ketothiolase (phaA), an acetoacetyl-coenzyme A reductase (phaB) and a putative transcriptional regulator (phaR). All genes were similar to pha genes from several related species, but differences were observed in the distal region of phaA. Complementation with heterologous β-ketothiolase genes from Azotobacter sp. FA8 or Pseudomonas putida GPp104 restored the capability of Pseudomonas sp. 14-3 to synthesize PHB from glucose, demonstrating that its β-ketothiolase was nonfunctional. Analysis of the genome sequences of other Pseudomonas species has revealed the existence of putative β-ketothiolase genes. The functionality of one of these thiolase genes, belonging to P. putida GPp104, was experimentally demonstrated. Pseudomonas sp. 14-3 is the first natural phaA mutant described, that despite this mutation accumulates high amounts of PHB when growing on fatty acids. © 2006 Federation of European Microbiological Societies.
Fil:Ayub, N.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Julia Pettinari, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Méndez, B.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. - Fuente
- FEMS Microbiol. Lett. 2006;264(1):125-131
- Materia
-
β-ketothiolase
Natural mutants
Polyhydroxybutyrate
Pseudomonas
acetyl coenzyme A acyltransferase
butyric acid derivative
polyhydroxybutyrate
unclassified drug
article
Azotobacter
biosynthesis
controlled study
gene expression
gene mutation
gene sequence
genetic analysis
molecular cloning
nonhuman
nucleotide sequence
phenotype
priority journal
Pseudomonas
Pseudomonas putida
transcription regulation
Acetyl-CoA C-Acyltransferase
Bacterial Proteins
Base Sequence
Cloning, Molecular
Genetic Complementation Test
Genome, Bacterial
Glucose
Hydroxybutyrates
Molecular Sequence Data
Octanoic Acids
Polyesters
Pseudomonas
Sequence Alignment
Azotobacter
Pseudomonas
Pseudomonas putida
Pseudomonas sp. 14-3 - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by/2.5/ar
- Repositorio
- Institución
- Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
- OAI Identificador
- paperaa:paper_03781097_v264_n1_p125_Ayub
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Impaired polyhydroxybutyrate biosynthesis from glucose in Pseudomonas sp. 14-3 is due to a defective β-ketothiolase geneAyub, N.D.Julia Pettinari, M.Méndez, B.S.López, N.I.β-ketothiolaseNatural mutantsPolyhydroxybutyratePseudomonasacetyl coenzyme A acyltransferasebutyric acid derivativepolyhydroxybutyrateunclassified drugarticleAzotobacterbiosynthesiscontrolled studygene expressiongene mutationgene sequencegenetic analysismolecular cloningnonhumannucleotide sequencephenotypepriority journalPseudomonasPseudomonas putidatranscription regulationAcetyl-CoA C-AcyltransferaseBacterial ProteinsBase SequenceCloning, MolecularGenetic Complementation TestGenome, BacterialGlucoseHydroxybutyratesMolecular Sequence DataOctanoic AcidsPolyestersPseudomonasSequence AlignmentAzotobacterPseudomonasPseudomonas putidaPseudomonas sp. 14-3Pseudomonas sp. 14-3 accumulates polyhydroxybutyrate (PHB) from octanoate, but not from glucose. To elucidate this unusual phenotype, genes responsible for the synthesis of PHB were cloned and analyzed. A PHB polymerase gene (phaC) was found downstream from genes coding for a β-ketothiolase (phaA), an acetoacetyl-coenzyme A reductase (phaB) and a putative transcriptional regulator (phaR). All genes were similar to pha genes from several related species, but differences were observed in the distal region of phaA. Complementation with heterologous β-ketothiolase genes from Azotobacter sp. FA8 or Pseudomonas putida GPp104 restored the capability of Pseudomonas sp. 14-3 to synthesize PHB from glucose, demonstrating that its β-ketothiolase was nonfunctional. Analysis of the genome sequences of other Pseudomonas species has revealed the existence of putative β-ketothiolase genes. The functionality of one of these thiolase genes, belonging to P. putida GPp104, was experimentally demonstrated. Pseudomonas sp. 14-3 is the first natural phaA mutant described, that despite this mutation accumulates high amounts of PHB when growing on fatty acids. © 2006 Federation of European Microbiological Societies.Fil:Ayub, N.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Julia Pettinari, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Méndez, B.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.2006info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12110/paper_03781097_v264_n1_p125_AyubFEMS Microbiol. Lett. 2006;264(1):125-131reponame:Biblioteca Digital (UBA-FCEN)instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesinstacron:UBA-FCENenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/ar2025-09-11T10:21:54Zpaperaa:paper_03781097_v264_n1_p125_AyubInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-09-11 10:21:55.656Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse |
dc.title.none.fl_str_mv |
Impaired polyhydroxybutyrate biosynthesis from glucose in Pseudomonas sp. 14-3 is due to a defective β-ketothiolase gene |
title |
Impaired polyhydroxybutyrate biosynthesis from glucose in Pseudomonas sp. 14-3 is due to a defective β-ketothiolase gene |
spellingShingle |
Impaired polyhydroxybutyrate biosynthesis from glucose in Pseudomonas sp. 14-3 is due to a defective β-ketothiolase gene Ayub, N.D. β-ketothiolase Natural mutants Polyhydroxybutyrate Pseudomonas acetyl coenzyme A acyltransferase butyric acid derivative polyhydroxybutyrate unclassified drug article Azotobacter biosynthesis controlled study gene expression gene mutation gene sequence genetic analysis molecular cloning nonhuman nucleotide sequence phenotype priority journal Pseudomonas Pseudomonas putida transcription regulation Acetyl-CoA C-Acyltransferase Bacterial Proteins Base Sequence Cloning, Molecular Genetic Complementation Test Genome, Bacterial Glucose Hydroxybutyrates Molecular Sequence Data Octanoic Acids Polyesters Pseudomonas Sequence Alignment Azotobacter Pseudomonas Pseudomonas putida Pseudomonas sp. 14-3 |
title_short |
Impaired polyhydroxybutyrate biosynthesis from glucose in Pseudomonas sp. 14-3 is due to a defective β-ketothiolase gene |
title_full |
Impaired polyhydroxybutyrate biosynthesis from glucose in Pseudomonas sp. 14-3 is due to a defective β-ketothiolase gene |
title_fullStr |
Impaired polyhydroxybutyrate biosynthesis from glucose in Pseudomonas sp. 14-3 is due to a defective β-ketothiolase gene |
title_full_unstemmed |
Impaired polyhydroxybutyrate biosynthesis from glucose in Pseudomonas sp. 14-3 is due to a defective β-ketothiolase gene |
title_sort |
Impaired polyhydroxybutyrate biosynthesis from glucose in Pseudomonas sp. 14-3 is due to a defective β-ketothiolase gene |
dc.creator.none.fl_str_mv |
Ayub, N.D. Julia Pettinari, M. Méndez, B.S. López, N.I. |
author |
Ayub, N.D. |
author_facet |
Ayub, N.D. Julia Pettinari, M. Méndez, B.S. López, N.I. |
author_role |
author |
author2 |
Julia Pettinari, M. Méndez, B.S. López, N.I. |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
β-ketothiolase Natural mutants Polyhydroxybutyrate Pseudomonas acetyl coenzyme A acyltransferase butyric acid derivative polyhydroxybutyrate unclassified drug article Azotobacter biosynthesis controlled study gene expression gene mutation gene sequence genetic analysis molecular cloning nonhuman nucleotide sequence phenotype priority journal Pseudomonas Pseudomonas putida transcription regulation Acetyl-CoA C-Acyltransferase Bacterial Proteins Base Sequence Cloning, Molecular Genetic Complementation Test Genome, Bacterial Glucose Hydroxybutyrates Molecular Sequence Data Octanoic Acids Polyesters Pseudomonas Sequence Alignment Azotobacter Pseudomonas Pseudomonas putida Pseudomonas sp. 14-3 |
topic |
β-ketothiolase Natural mutants Polyhydroxybutyrate Pseudomonas acetyl coenzyme A acyltransferase butyric acid derivative polyhydroxybutyrate unclassified drug article Azotobacter biosynthesis controlled study gene expression gene mutation gene sequence genetic analysis molecular cloning nonhuman nucleotide sequence phenotype priority journal Pseudomonas Pseudomonas putida transcription regulation Acetyl-CoA C-Acyltransferase Bacterial Proteins Base Sequence Cloning, Molecular Genetic Complementation Test Genome, Bacterial Glucose Hydroxybutyrates Molecular Sequence Data Octanoic Acids Polyesters Pseudomonas Sequence Alignment Azotobacter Pseudomonas Pseudomonas putida Pseudomonas sp. 14-3 |
dc.description.none.fl_txt_mv |
Pseudomonas sp. 14-3 accumulates polyhydroxybutyrate (PHB) from octanoate, but not from glucose. To elucidate this unusual phenotype, genes responsible for the synthesis of PHB were cloned and analyzed. A PHB polymerase gene (phaC) was found downstream from genes coding for a β-ketothiolase (phaA), an acetoacetyl-coenzyme A reductase (phaB) and a putative transcriptional regulator (phaR). All genes were similar to pha genes from several related species, but differences were observed in the distal region of phaA. Complementation with heterologous β-ketothiolase genes from Azotobacter sp. FA8 or Pseudomonas putida GPp104 restored the capability of Pseudomonas sp. 14-3 to synthesize PHB from glucose, demonstrating that its β-ketothiolase was nonfunctional. Analysis of the genome sequences of other Pseudomonas species has revealed the existence of putative β-ketothiolase genes. The functionality of one of these thiolase genes, belonging to P. putida GPp104, was experimentally demonstrated. Pseudomonas sp. 14-3 is the first natural phaA mutant described, that despite this mutation accumulates high amounts of PHB when growing on fatty acids. © 2006 Federation of European Microbiological Societies. Fil:Ayub, N.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Julia Pettinari, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Méndez, B.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. |
description |
Pseudomonas sp. 14-3 accumulates polyhydroxybutyrate (PHB) from octanoate, but not from glucose. To elucidate this unusual phenotype, genes responsible for the synthesis of PHB were cloned and analyzed. A PHB polymerase gene (phaC) was found downstream from genes coding for a β-ketothiolase (phaA), an acetoacetyl-coenzyme A reductase (phaB) and a putative transcriptional regulator (phaR). All genes were similar to pha genes from several related species, but differences were observed in the distal region of phaA. Complementation with heterologous β-ketothiolase genes from Azotobacter sp. FA8 or Pseudomonas putida GPp104 restored the capability of Pseudomonas sp. 14-3 to synthesize PHB from glucose, demonstrating that its β-ketothiolase was nonfunctional. Analysis of the genome sequences of other Pseudomonas species has revealed the existence of putative β-ketothiolase genes. The functionality of one of these thiolase genes, belonging to P. putida GPp104, was experimentally demonstrated. Pseudomonas sp. 14-3 is the first natural phaA mutant described, that despite this mutation accumulates high amounts of PHB when growing on fatty acids. © 2006 Federation of European Microbiological Societies. |
publishDate |
2006 |
dc.date.none.fl_str_mv |
2006 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/20.500.12110/paper_03781097_v264_n1_p125_Ayub |
url |
http://hdl.handle.net/20.500.12110/paper_03781097_v264_n1_p125_Ayub |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
http://creativecommons.org/licenses/by/2.5/ar |
dc.format.none.fl_str_mv |
application/pdf |
dc.source.none.fl_str_mv |
FEMS Microbiol. Lett. 2006;264(1):125-131 reponame:Biblioteca Digital (UBA-FCEN) instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales instacron:UBA-FCEN |
reponame_str |
Biblioteca Digital (UBA-FCEN) |
collection |
Biblioteca Digital (UBA-FCEN) |
instname_str |
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales |
instacron_str |
UBA-FCEN |
institution |
UBA-FCEN |
repository.name.fl_str_mv |
Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales |
repository.mail.fl_str_mv |
ana@bl.fcen.uba.ar |
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1842975013538365440 |
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13.004268 |