The gluconeogenic enzyme fructose-1,6-bisphosphatase is dispensable for growth of the yeast yarrowia lipolytica in gluconeogenic substrates

The genes encoding gluconeogenic enzymes in the nonconventional yeast Yarrowia lipolytica were found to be differentially regulated. The expression of Y. lipolytica FBP1 (YlFBP1) encoding the key enzyme fructose-1,6-bisphosphatase was not repressed by glucose in contrast with the situation in other...

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Detalles Bibliográficos
Autores: Jardón, Raquel, Gancedo, Carlos, Flores, Carmen-Lisset
Tipo de recurso: artículo
Fecha de publicación:2008
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/22136
Acceso en línea:http://hdl.handle.net/10261/22136
Access Level:acceso abierto
Palabra clave:Carbon catabolite repression
Saccharomyces-cerevisiae
Glucose repression
Isocitrate lyase
Fructose 1,6-bisphosphatase
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spelling The gluconeogenic enzyme fructose-1,6-bisphosphatase is dispensable for growth of the yeast yarrowia lipolytica in gluconeogenic substratesJardón, RaquelGancedo, CarlosFlores, Carmen-LissetCarbon catabolite repressionSaccharomyces-cerevisiaeGlucose repressionIsocitrate lyaseFructose 1,6-bisphosphataseThe genes encoding gluconeogenic enzymes in the nonconventional yeast Yarrowia lipolytica were found to be differentially regulated. The expression of Y. lipolytica FBP1 (YlFBP1) encoding the key enzyme fructose-1,6-bisphosphatase was not repressed by glucose in contrast with the situation in other yeasts; however, this sugar markedly repressed the expression of YlPCK1, encoding phosphoenolpyruvate carboxykinase, and YlICL1, encoding isocitrate lyase. We constructed Y. lipolytica strains with two different disrupted versions of YlFBP1 and found that they grew much slower than the wild type in gluconeogenic carbon sources but that growth was not abolished as happens in most microorganisms. We attribute this growth to the existence of an alternative phosphatase with a high Km (2.3 mM) for fructose-1,6-bisphosphate. The gene YlFBP1 restored fructose-1,6-bisphosphatase activity and growth in gluconeogenic carbon sources to a Saccharomyces cerevisiae fbp1 mutant, but the introduction of the FBP1 gene from S. cerevisiae in the Ylfbp1 mutant did not produce fructose-1,6-bisphosphatase activity or growth complementation. Subcellular fractionation revealed the presence of fructose-1,6-bisphosphatase both in the cytoplasm and in the nucleus.Spanish Direccion General de Investigacion Cientfica y Tecnica - BFU 2004-02855-C02-1 Formacion de Profesorado Universitario Spanish Ministerio de Educacion y Ciencia.Peer reviewedAmerican Society for Microbiology201020102008info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_65011011634 bytesapplication/pdfhttp://hdl.handle.net/10261/22136reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1128/EC.00169-08info:eu-repo/semantics/openAccessoai:digital.csic.es:10261/221362026-05-22T06:33:51Z
dc.title.none.fl_str_mv The gluconeogenic enzyme fructose-1,6-bisphosphatase is dispensable for growth of the yeast yarrowia lipolytica in gluconeogenic substrates
title The gluconeogenic enzyme fructose-1,6-bisphosphatase is dispensable for growth of the yeast yarrowia lipolytica in gluconeogenic substrates
spellingShingle The gluconeogenic enzyme fructose-1,6-bisphosphatase is dispensable for growth of the yeast yarrowia lipolytica in gluconeogenic substrates
Jardón, Raquel
Carbon catabolite repression
Saccharomyces-cerevisiae
Glucose repression
Isocitrate lyase
Fructose 1,6-bisphosphatase
title_short The gluconeogenic enzyme fructose-1,6-bisphosphatase is dispensable for growth of the yeast yarrowia lipolytica in gluconeogenic substrates
title_full The gluconeogenic enzyme fructose-1,6-bisphosphatase is dispensable for growth of the yeast yarrowia lipolytica in gluconeogenic substrates
title_fullStr The gluconeogenic enzyme fructose-1,6-bisphosphatase is dispensable for growth of the yeast yarrowia lipolytica in gluconeogenic substrates
title_full_unstemmed The gluconeogenic enzyme fructose-1,6-bisphosphatase is dispensable for growth of the yeast yarrowia lipolytica in gluconeogenic substrates
title_sort The gluconeogenic enzyme fructose-1,6-bisphosphatase is dispensable for growth of the yeast yarrowia lipolytica in gluconeogenic substrates
dc.creator.none.fl_str_mv Jardón, Raquel
Gancedo, Carlos
Flores, Carmen-Lisset
author Jardón, Raquel
author_facet Jardón, Raquel
Gancedo, Carlos
Flores, Carmen-Lisset
author_role author
author2 Gancedo, Carlos
Flores, Carmen-Lisset
author2_role author
author
dc.subject.none.fl_str_mv Carbon catabolite repression
Saccharomyces-cerevisiae
Glucose repression
Isocitrate lyase
Fructose 1,6-bisphosphatase
topic Carbon catabolite repression
Saccharomyces-cerevisiae
Glucose repression
Isocitrate lyase
Fructose 1,6-bisphosphatase
description The genes encoding gluconeogenic enzymes in the nonconventional yeast Yarrowia lipolytica were found to be differentially regulated. The expression of Y. lipolytica FBP1 (YlFBP1) encoding the key enzyme fructose-1,6-bisphosphatase was not repressed by glucose in contrast with the situation in other yeasts; however, this sugar markedly repressed the expression of YlPCK1, encoding phosphoenolpyruvate carboxykinase, and YlICL1, encoding isocitrate lyase. We constructed Y. lipolytica strains with two different disrupted versions of YlFBP1 and found that they grew much slower than the wild type in gluconeogenic carbon sources but that growth was not abolished as happens in most microorganisms. We attribute this growth to the existence of an alternative phosphatase with a high Km (2.3 mM) for fructose-1,6-bisphosphate. The gene YlFBP1 restored fructose-1,6-bisphosphatase activity and growth in gluconeogenic carbon sources to a Saccharomyces cerevisiae fbp1 mutant, but the introduction of the FBP1 gene from S. cerevisiae in the Ylfbp1 mutant did not produce fructose-1,6-bisphosphatase activity or growth complementation. Subcellular fractionation revealed the presence of fructose-1,6-bisphosphatase both in the cytoplasm and in the nucleus.
publishDate 2008
dc.date.none.fl_str_mv 2008
2010
2010
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/22136
url http://hdl.handle.net/10261/22136
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.1128/EC.00169-08
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 1011634 bytes
application/pdf
dc.publisher.none.fl_str_mv American Society for Microbiology
publisher.none.fl_str_mv American Society for Microbiology
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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