A new family of enzymes catalyzing the first committed step of the methylerythritol 4-phosphate (MEP) pathway for isoprenoid biosynthesis in bacteria

6 pages, 4 figures, 1 table.

Detalles Bibliográficos
Autores: Sangari, Félix J., Pérez-Gil, Jordi, Carretero-Paulet, Lorenzo, García-Lobo, Juan M., Rodriguez-Concepcion, Manuel
Tipo de recurso: artículo
Fecha de publicación:2010
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/28717
Acceso en línea:http://hdl.handle.net/10261/28717
Access Level:acceso abierto
Palabra clave:Brucella
DXR
Fosmidomycin
Methylerythritol
Phylogenetic
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spelling A new family of enzymes catalyzing the first committed step of the methylerythritol 4-phosphate (MEP) pathway for isoprenoid biosynthesis in bacteriaSangari, Félix J.Pérez-Gil, JordiCarretero-Paulet, LorenzoGarcía-Lobo, Juan M.Rodriguez-Concepcion, ManuelBrucellaDXRFosmidomycinMethylerythritolPhylogenetic6 pages, 4 figures, 1 table.Isoprenoids are a large family of compounds with essential functions in all domains of life. Most eubacteria synthesize their isoprenoids using the methylerythritol 4-phosphate (MEP) pathway, whereas a minority uses the unrelated mevalonate pathway and only a few have both. Interestingly, Brucella abortus and some other bacteria that only use the MEP pathway lack deoxyxylulose 5-phosphate (DXP) reductoisomerase (DXR), the enzyme catalyzing the NADPH-dependent production of MEP from DXP in the first committed step of the pathway. Fosmidomycin, a specific competitive inhibitor of DXR, inhibited growth of B. abortus cells expressing the Escherichia coli GlpT transporter (required for fosmidomycin uptake), confirming that a DXR-like (DRL) activity exists in these bacteria. The B. abortus DRL protein was found to belong to a family of uncharacterized proteins similar to homoserine dehydrogenase. Subsequent experiments confirmed that DRL and DXR catalyze the same biochemical reaction. DRL homologues shown to complement a DXR-deficient E. coli strain grouped within the same phylogenetic clade. The scattered taxonomic distribution of sequences from the DRL clade and the occurrence of several paralogues in some bacterial strains might be the result of lateral gene transfer and lineage-specific gene duplications and/or losses, similar to that described for typical mevalonate and MEP pathway genes. These results reveal the existence of a novel class of oxidoreductases catalyzing the conversion of DXP into MEP in prokaryotic cells, underscoring the biochemical and genetic plasticity achieved by bacteria to synthesize essential compounds such as isoprenoids.The Spanish Ministerio de Ciencia e Innovación provided a PhD fellowship to J.P.-G., a Juan de la Cierva contract to L.C.-P. (cofinanced by the European Social Fund), research Grants BIO2007-63656 to F.J.S. and BIO2008-00432 to M.R.-C., as well as funding through a Consolider program (CSD2007-00036). This work was also supported by grants from the Fundación Marqués de Valdecilla (API 07∕01) to F.J.S., and the Generalitat de Catalunya (SGR and XaRBa) to M.R.-C.Peer reviewedNational Academy of Sciences (U.S.)201020102010info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501http://hdl.handle.net/10261/28717reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1073/pnas.1001962107info:eu-repo/semantics/openAccessoai:digital.csic.es:10261/287172026-05-22T06:33:51Z
dc.title.none.fl_str_mv A new family of enzymes catalyzing the first committed step of the methylerythritol 4-phosphate (MEP) pathway for isoprenoid biosynthesis in bacteria
title A new family of enzymes catalyzing the first committed step of the methylerythritol 4-phosphate (MEP) pathway for isoprenoid biosynthesis in bacteria
spellingShingle A new family of enzymes catalyzing the first committed step of the methylerythritol 4-phosphate (MEP) pathway for isoprenoid biosynthesis in bacteria
Sangari, Félix J.
Brucella
DXR
Fosmidomycin
Methylerythritol
Phylogenetic
title_short A new family of enzymes catalyzing the first committed step of the methylerythritol 4-phosphate (MEP) pathway for isoprenoid biosynthesis in bacteria
title_full A new family of enzymes catalyzing the first committed step of the methylerythritol 4-phosphate (MEP) pathway for isoprenoid biosynthesis in bacteria
title_fullStr A new family of enzymes catalyzing the first committed step of the methylerythritol 4-phosphate (MEP) pathway for isoprenoid biosynthesis in bacteria
title_full_unstemmed A new family of enzymes catalyzing the first committed step of the methylerythritol 4-phosphate (MEP) pathway for isoprenoid biosynthesis in bacteria
title_sort A new family of enzymes catalyzing the first committed step of the methylerythritol 4-phosphate (MEP) pathway for isoprenoid biosynthesis in bacteria
dc.creator.none.fl_str_mv Sangari, Félix J.
Pérez-Gil, Jordi
Carretero-Paulet, Lorenzo
García-Lobo, Juan M.
Rodriguez-Concepcion, Manuel
author Sangari, Félix J.
author_facet Sangari, Félix J.
Pérez-Gil, Jordi
Carretero-Paulet, Lorenzo
García-Lobo, Juan M.
Rodriguez-Concepcion, Manuel
author_role author
author2 Pérez-Gil, Jordi
Carretero-Paulet, Lorenzo
García-Lobo, Juan M.
Rodriguez-Concepcion, Manuel
author2_role author
author
author
author
dc.subject.none.fl_str_mv Brucella
DXR
Fosmidomycin
Methylerythritol
Phylogenetic
topic Brucella
DXR
Fosmidomycin
Methylerythritol
Phylogenetic
description 6 pages, 4 figures, 1 table.
publishDate 2010
dc.date.none.fl_str_mv 2010
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/10261/28717
url http://hdl.handle.net/10261/28717
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.1073/pnas.1001962107
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv National Academy of Sciences (U.S.)
publisher.none.fl_str_mv National Academy of Sciences (U.S.)
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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score 15,811543

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