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  2. FCEN
  3. FCEN - Facultad de Ciencias Exactas y Naturales. UBA
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dc.provenanceFacultad de Ciencias Exactas y Naturales de la UBA-
dc.contributor<div class="autor_fcen" id="27">Acevedo, J.M.</div>-
dc.contributor<div class="autor_fcen" id="1746">Centanin, L.</div>-
dc.contributor<div class="autor_fcen" id="2422">Dekanty, A.</div>-
dc.contributor<div class="autor_fcen" id="9128">Wappner, P.</div>-
dc.creator<div class="autor_fcen" id="27">Acevedo, J.M.</div>-
dc.creator<div class="autor_fcen" id="1746">Centanin, L.</div>-
dc.creator<div class="autor_fcen" id="2422">Dekanty, A.</div>-
dc.creator<div class="autor_fcen" id="9128">Wappner, P.</div>-
dc.date.accessioned2018-05-04T22:08:32Z-
dc.date.accessioned2018-05-28T15:49:02Z-
dc.date.available2018-05-04T22:08:32Z-
dc.date.available2018-05-28T15:49:02Z-
dc.date.issued2010-
dc.identifier.urihttp://10.0.0.11:8080/jspui/handle/bnmm/68599-
dc.descriptionBackground: The Hypoxia Inducible Factor (HIF) mediates cellular adaptations to low oxygen. Prolyl-4-hydroxylases are oxygen sensors that hydroxylate the HIF alpha-subunit, promoting its proteasomal degradation in normoxia. Three HIFprolyl hydroxylases, encoded by independent genes, PHD1, PHD2, and PHD3, occur in mammals. PHD2, the longest PHD isoform includes a MYND domain, whose biochemical function is unclear. PHD2 and PHD3 genes are induced in hypoxia to shut down HIF dependent transcription upon reoxygenation, while expression of PHD1 is oxygen-independent. The physiologic significance of the diversity of the PHD oxygen sensors is intriguing. Methodology and Principal Findings: We have analyzed the Drosophila PHD locus, fatiga, which encodes 3 isoforms, FgaA, FgaB and FgaC that are originated through a combination of alternative initiation of transcription and alternative splicing. FgaA includes a MYND domain and is homologous to PHD2, while FgaB and FgaC are shorter isoforms most similar to PHD3. Through a combination of genetic experiments in vivo and molecular analyses in cell culture, we show that fgaB but not fgaA is induced in hypoxia, in a Sima-dependent manner, through a HIF-Responsive Element localized in the first intron of fgaA. The regulatory capacity of FgaB is stronger than that of FgaA, as complete reversion of fga loss-of-function phenotypes is observed upon transgenic expression of the former, and only partial rescue occurs after expression of the latter. Conclusions and Significance: Diversity of PHD isoforms is a conserved feature in evolution. As in mammals, there are hypoxia-inducible and non-inducible Drosophila PHDs, and a fly isoform including a MYND domain co-exists with isoforms lacking this domain. Our results suggest that the isoform devoid of a MYND domain has stronger regulatory capacity than that including this domain.-
dc.descriptionFil:Acevedo, J.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.-
dc.descriptionFil:Centanin, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.-
dc.descriptionFil:Dekanty, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.-
dc.descriptionFil:Wappner, P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.-
dc.formatapplication/pdf-
dc.languageeng-
dc.rightsinfo:eu-repo/semantics/openAccess-
dc.rightshttp://creativecommons.org/licenses/by/2.5/ar-
dc.sourcePLoS ONE 2010;5(8)-
dc.source.urihttp://digital.bl.fcen.uba.ar/Download/paper/paper_19326203_v5_n8_p_Acevedo.pdf-
dc.subjecthypoxia inducible factor-
dc.subjectoxygenase-
dc.subjectpolyhistidine tag-
dc.subjectprocollagen proline 2 oxoglutarate 4 dioxygenase-
dc.subjectprolyl 4 hydroxylase 1-
dc.subjectprolyl 4 hydroxylase 2-
dc.subjectprolyl 4 hydroxylase 3-
dc.subjectunclassified drug-
dc.subjectDNA binding protein-
dc.subjectDrosophila protein-
dc.subjectisoenzyme-
dc.subjectmessenger RNA-
dc.subjectoxygen-
dc.subjectSima protein, Drosophila-
dc.subjectalternative RNA splicing-
dc.subjectanimal cell-
dc.subjectarticle-
dc.subjectcell hypoxia-
dc.subjectcontrolled study-
dc.subjectDrosophila-
dc.subjectembryo-
dc.subjectgene expression regulation-
dc.subjectgene locus-
dc.subjectgene overexpression-
dc.subjectimago-
dc.subjectin vivo study-
dc.subjectinsect cell culture-
dc.subjectintron-
dc.subjectloss of function mutation-
dc.subjectmolecular dynamics-
dc.subjectnonhuman-
dc.subjectoxygen sensing-
dc.subjectphenotypic variation-
dc.subjectprotein domain-
dc.subjectprotein localization-
dc.subjecttranscription initiation site-
dc.subjecttransgenics-
dc.subjectanimal-
dc.subjectanoxia-
dc.subjectchemistry-
dc.subjectDNA responsive element-
dc.subjectDrosophila melanogaster-
dc.subjectenzymology-
dc.subjectgenetics-
dc.subjectgrowth, development and aging-
dc.subjecthuman-
dc.subjectlife cycle-
dc.subjectmetabolism-
dc.subjectprotein tertiary structure-
dc.subjectupregulation-
dc.subjectMammalia-
dc.subjectAlternative Splicing-
dc.subjectAnimals-
dc.subjectAnoxia-
dc.subjectDNA-Binding Proteins-
dc.subjectDrosophila melanogaster-
dc.subjectDrosophila Proteins-
dc.subjectGene Expression Regulation, Enzymologic-
dc.subjectGenetic Loci-
dc.subjectHumans-
dc.subjectIsoenzymes-
dc.subjectLife Cycle Stages-
dc.subjectOxygen-
dc.subjectProcollagen-Proline Dioxygenase-
dc.subjectProtein Structure, Tertiary-
dc.subjectResponse Elements-
dc.subjectRNA, Messenger-
dc.subjectUp-Regulation-
dc.titleOxygen sensing in Drosophila: Multiple isoforms of the prolyl hydroxylase fatiga have different capacity to regulate HIFαSima-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:ar-repo/semantics/artículo-
dc.typeinfo:eu-repo/semantics/publishedVersion-
Aparece en las colecciones: FCEN - Facultad de Ciencias Exactas y Naturales. UBA

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