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dc.contributor.authorWong Sak Hoi, Joanne
dc.contributor.authorLamarre, Claude
dc.contributor.authorBeau, Rémi
dc.contributor.authorMeneau, Isabelle
dc.contributor.authorBerepiki, Adokiye
dc.contributor.authorBarre, Annick
dc.contributor.authorMellado, Emilia 
dc.contributor.authorRead, Nick D
dc.contributor.authorLatgé, Jean-Paul
dc.date.accessioned2018-12-17T14:36:58Z
dc.date.available2018-12-17T14:36:58Z
dc.date.issued2011-06-01
dc.identifier.citationMol Biol Cell. 2011;22(11):1896-906.es_ES
dc.identifier.urihttp://hdl.handle.net/20.500.12105/6881
dc.description.abstractDuring a search for genes controlling conidial dormancy in Aspergillus fumigatus, two dehydrin-like genes, DprA and DprB, were identified. The deduced proteins had repeated stretches of 23 amino acids that contained a conserved dehydrin-like protein (DPR) motif. Disrupted DprAΔ mutants were hypersensitive to oxidative stress and to phagocytic killing, whereas DprBΔ mutants were impaired in osmotic and pH stress responses. However, no effect was observed on their pathogenicity in our experimental models of invasive aspergillosis. Molecular dissection of the signaling pathways acting upstream showed that expression of DprA was dependent on the stress-activated kinase SakA and the cyclic AMP-protein kinase A (cAMP-PKA) pathways, which activate the bZIP transcription factor AtfA, while expression of DprB was dependent on the SakA mitogen-activated protein kinase (MAPK) pathway, and the zinc finger transcription factor PacC. Fluorescent protein fusions showed that both proteins were associated with peroxisomes and the cytosol. Accordingly, DprA and DprB were important for peroxisome function. Our findings reveal a novel family of stress-protective proteins in A. fumigatus and, potentially, in filamentous ascomycetes.es_ES
dc.language.isoenges_ES
dc.publisherAmerican Society for Cell Biology (ASCB) es_ES
dc.type.hasVersionVoRes_ES
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/3.0/*
dc.subject.meshAmino Acid Sequence es_ES
dc.subject.meshAnimals es_ES
dc.subject.meshAspergillosis es_ES
dc.subject.meshAspergillus fumigatus es_ES
dc.subject.meshCatalase es_ES
dc.subject.meshDithiothreitol es_ES
dc.subject.meshEnzyme Assays es_ES
dc.subject.meshFungal Proteins es_ES
dc.subject.meshGene Expression Regulation, Fungal es_ES
dc.subject.meshHumans es_ES
dc.subject.meshHydrogen-Ion Concentration es_ES
dc.subject.meshMAP Kinase Signaling System es_ES
dc.subject.meshMice es_ES
dc.subject.meshMolecular Chaperones es_ES
dc.subject.meshMolecular Sequence Data es_ES
dc.subject.meshOsmotic Pressure es_ES
dc.subject.meshOxidation-Reduction es_ES
dc.subject.meshPeroxisomes es_ES
dc.subject.meshPhenotype es_ES
dc.subject.meshSequence Alignment es_ES
dc.subject.meshSequence Deletion es_ES
dc.subject.meshSpores, Fungal es_ES
dc.subject.meshStress, Physiological es_ES
dc.subject.meshTranscription, Genetices_ES
dc.subject.meshUnfolded Protein Response es_ES
dc.titleA novel family of dehydrin-like proteins is involved in stress response in the human fungal pathogen Aspergillus fumigatuses_ES
dc.typejournal articlees_ES
dc.rights.licenseAtribución-NoComercial-CompartirIgual 3.0*
dc.identifier.pubmedID21490150es_ES
dc.format.volume22es_ES
dc.format.number11es_ES
dc.format.page1896-906es_ES
dc.identifier.doi10.1091/mbc.E10-11-0914es_ES
dc.description.peerreviewedes_ES
dc.identifier.e-issn1939-4586es_ES
dc.relation.publisherversionhttps://www.doi.org/10.1091/mbc.E10-11-0914es_ES
dc.identifier.journalMolecular biology of the celles_ES
dc.repisalud.centroISCIII::Centro Nacional de Microbiologíaes_ES
dc.repisalud.institucionISCIIIes_ES
dc.rights.accessRightsopen accesses_ES


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