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Phylogenetic and genetic linkage between novel atypical dual-specificity phosphatases from non-metazoan organisms

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Phylogenetic and genetic linkage between novel atypical dual-specificity phosphatases from non-metazoan organisms

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dc.contributor.author Romá-Mateo, C es_ES
dc.contributor.author Sacristán-Reviriego, A es_ES
dc.contributor.author Beresford, N.J es_ES
dc.contributor.author Caparrós Martín, José Antonio es_ES
dc.contributor.author Culiañez Macia, Francisco Antonio es_ES
dc.contributor.author Martin, H es_ES
dc.contributor.author Molina, M es_ES
dc.contributor.author Tabernero, L es_ES
dc.contributor.author Pulido, R es_ES
dc.date.accessioned 2017-07-17T09:41:40Z
dc.date.available 2017-07-17T09:41:40Z
dc.date.issued 2011-04
dc.identifier.issn 1617-4615
dc.identifier.uri http://hdl.handle.net/10251/85242
dc.description.abstract [EN] Dual-specificity phosphatases (DSPs) constitute a large protein tyrosine phosphatase (PTP) family, with examples in distant evolutive phyla. PFA-DSPs (Plant and Fungi Atypical DSPs) are a group of atypical DSPs present in plants, fungi, kinetoplastids, and slime molds, the members of which share structural similarity with atypical- and lipid phosphatase DSPs from mammals. The analysis of the PFA-DSPs from the plant Arabidopsis thaliana (AtPFA-DSPs) showed differential tissue mRNA expression, substrate specificity, and catalytic activity for these proteins, suggesting different functional roles among plant PFA-DSPs. Bioinformatic analysis revealed the existence of novel PFA-DSP-related proteins in fungi (Oca1, Oca2, Oca4 and Oca6 in Saccharomyces cerevisiae) and protozoa, which were segregated from plant PFADSPs. The closest yeast homolog for these proteins was the PFA-DSP from S. cerevisiae ScPFA-DSP1/Siw14/Oca3. Oca1, Oca2, Siw14/Oca3, Oca4, and Oca6 were involved in the yeast response to caffeine and rapamycin stresses. Siw14/Oca3 was an active phosphatase in vitro, whereas no phosphatase activity could be detected for Oca1. Remarkably, overexpression of Siw14/Oca3 suppressed the caffeine sensitivity of oca1, oca2, oca4, and oca6 deleted strains, indicating a genetic linkage and suggesting a functional relationship for these proteins. Functional studies on mutations targeting putative catalytic residues from the A. thaliana AtPFA-DSP1/At1g05000 protein indicated the absence of canonical amino acids acting as the general acid/base in the phosphor-ester hydrolysis, which suggests a specific mechanism of reaction for PFA-DSPs and related enzymes. Our studies demonstrate the existence of novel phosphatase protein families in fungi and protozoa, with active and inactive enzymes linked in common signaling pathways. This illustrates the catalytic and functional complexity of the expanding family of atypical dual-specificity phosphatases in non-metazoans, including parasite organisms responsible for infectious human diseases. es_ES
dc.description.sponsorship This work was supported in part by grants SAF2006-08319 from Ministerio de Educacion y Ciencia, SAF2009-10226 from Ministerio de Ciencia e Innovacion (Spain and Fondo Europeo de Desarrollo Regional, FEDER; Plan de estimulo a la economia y el empleo, Plan E), AP-117/08, ACOMP2009/363 and ACOMP2010/222 from Generalitat Valenciana (Spain) (to R. P.), G0701233 from Medical Research Council (U.K.) (to L. T.), BIO2007-67299 from Ministerio de Ciencia e Innovacion (Spain) (to M. M.), and by European Union Research Training Network MRTN-CT-2006-035830. C. Roma-Mateo and A. Sacristan-Reviriego have been recipients of predoctoral fellowships from Ministerio de Educacion y Ciencia (Spain). We thank Peter Sudbery and Jose Luis Revuelta for providing cDNAs, the Arabidopsis Biological Resource Center (USA; donors: SSP Consortium, Sakis Theologis, Joe Ecker) for providing plasmids, and Isabel Rogla and Charis Saville for expert technical assistance.
dc.language Inglés es_ES
dc.publisher Springer Verlag (Germany) es_ES
dc.relation info:eu-repo/grantAgreement/MEC//SAF2006-08319/ES/MECANISMOS DE CONTROL CELULAR A TRAVES DEL SUPRESOR TUMORAL PTEN Y PTPS DUALES ESPECIFICAS DE MAP QUINASAS/ es_ES
dc.relation info:eu-repo/grantAgreement/MICINN//SAF2009-10226/ES/Implicacion De Nuevas Familias De Fosfatasas Y Quinasas En Cancer Y Neurodegeneracion/ es_ES
dc.relation GV/ACOMP2009/363 es_ES
dc.relation EC/MRTN-CT-2006-035830 es_ES
dc.relation info:eu-repo/grantAgreement/MEC//BIO2007-67299/ES/ANALISIS GLOBAL DE LA REGULACION NEGATIVA DE RUTAS DE MAPKS Y CARACTERIZACION DE PROTEINAS DE VIRULENCIA DE SALMONELLA Y BURKHOLDERIA EN EL MODELO EUCARIOTICO DE SEÑALIZACION SACCHAROMYCES CEREVISIAE/
dc.relation GV/ACOMP2010/222
dc.relation info:eu-repo/grantAgreement/Generalitat Valenciana//AP-117%2F08/ES/Caracterización molecular y funcional de proteínas fosfatasas de especificidad dual implicadas en neurodegeneración y cáncer./
dc.relation MRC/G0701233
dc.relation.ispartof Molecular Genetics and Genomics es_ES
dc.rights Reserva de todos los derechos es_ES
dc.subject Phosphatase es_ES
dc.subject Phosphorylation es_ES
dc.title Phylogenetic and genetic linkage between novel atypical dual-specificity phosphatases from non-metazoan organisms es_ES
dc.type Artículo es_ES
dc.identifier.doi 10.1007/ s00438-011-0611-6
dc.rights.accessRights Cerrado es_ES
dc.contributor.affiliation Universitat Politècnica de València. Instituto Universitario Mixto de Biología Molecular y Celular de Plantas - Institut Universitari Mixt de Biologia Molecular i Cel·lular de Plantes es_ES
dc.description.bibliographicCitation Romá-Mateo, C.; Sacristán-Reviriego, A.; Beresford, N.; Caparrós Martín, JA.; Culiañez Macia, FA.; Martin, H.; Molina, M.... (2011). Phylogenetic and genetic linkage between novel atypical dual-specificity phosphatases from non-metazoan organisms. Molecular Genetics and Genomics. 285(4):341-354. https://doi.org/10.1007/ s00438-011-0611-6 es_ES
dc.description.accrualMethod S es_ES
dc.relation.publisherversion http://doi.org/10.1007/s00438-011-0611-6 es_ES
dc.description.upvformatpinicio 341 es_ES
dc.description.upvformatpfin 354 es_ES
dc.type.version info:eu-repo/semantics/publishedVersion es_ES
dc.description.volume 285 es_ES
dc.description.issue 4 es_ES
dc.relation.senia 213012 es_ES
dc.identifier.pmid 21409566
dc.contributor.funder Ministerio de Educación y Ciencia
dc.contributor.funder Ministerio de Ciencia e Innovación
dc.contributor.funder European Commission
dc.contributor.funder Generalitat Valenciana
dc.contributor.funder Medical Research Council, Reino Unido
dc.contributor.funder European Regional Development Fund


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