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dc.contributor.authorMartín-Montalvo, Alejandroes_ES
dc.contributor.authorGonzález-Mariscal, Isabeles_ES
dc.contributor.authorPadilla, Sergioes_ES
dc.contributor.authorBallesteros, Manueles_ES
dc.contributor.authorBrautigan, David L.es_ES
dc.contributor.authorNavas, Plácidoes_ES
dc.contributor.authorSantos-Ocaña, Carloses_ES
dc.date.accessioned2016-02-10T10:09:03Z-
dc.date.available2016-02-10T10:09:03Z-
dc.date.issued2011-
dc.identifier.citationBiochemical Journal 440(1): 107-114 (2011)es_ES
dc.identifier.issn0264-6021-
dc.identifier.urihttp://hdl.handle.net/10261/128944-
dc.description.abstractCoQ6 (coenzyme Q6) biosynthesis in yeast is a well-regulated process that requires the final conversion of the late intermediate DMQ6 (demethoxy-CoQ6) into CoQ6 in order to support respiratory metabolism in yeast. The gene CAT5/COQ7 encodes the Cat5/Coq7 protein that catalyses the hydroxylation step of DMQ6 conversion into CoQ6. In the present study, we demonstrated that yeast Coq7 recombinant protein purified in bacteria can be phosphorylated in vitro using commercial PKA (protein kinase A) or PKC (protein kinase C) at the predicted amino acids Ser20, Ser28 and Thr32. The total absence of phosphorylation in a Coq7p version containing alanine instead of these phospho-amino acids, the high extent of phosphorylation produced and the saturated conditions maintained in the phosphorylation assay indicate that probably no other putative amino acids are phosphorylated in Coq7p. Results from in vitro assays have been corroborated using phosphorylation assays performed in purified mitochondria without external or commercial kinases. Coq7p remains phosphorylated in fermentative conditions and becomes dephosphorylated when respiratory metabolism is induced. The substitution of phosphorylated residues to alanine dramatically increases CoQ6 levels (256%). Conversely, substitution with negatively charged residues decreases CoQ6 content (57%). These modifications produced in Coq7p also alter the ratio between DMQ6 and CoQ6 itself, indicating that the Coq7p phosphorylation state is a regulatory mechanism for CoQ6 synthesis.es_ES
dc.description.sponsorshipThis work was supported by the Spanish Ministerio de Ciencia y Tecnología [grant number FIS PI080500]; the Junta de Andalucía [grant number P08-CTS-03988]; and by a grant from the International Q10 Association entitled “Phosphorylation-based regulation of coenzyme Q biosynthesis in yeast”. A.M.-M. received a predoctoral fellowship from the Consejer´ıa de Innovacion Ciencia y Empresa, Junta de Andalucía (Spain). I.G.-M. received a predoctoral fellowship from the Plan Propio of the Universidad Pablo de Olavide de Sevilla.es_ES
dc.language.isoenges_ES
dc.publisherBiochemical Societyes_ES
dc.rightsclosedAccesses_ES
dc.subjectCoenzyme Qes_ES
dc.subjectMitochondriones_ES
dc.subjectPhosphorylationes_ES
dc.subjectRespirationes_ES
dc.subjectYeastes_ES
dc.titleRespiratory-induced coenzyme Q biosynthesis is regulated by a phosphorylation cycle of Cat5p/Coq7pes_ES
dc.typeartículoes_ES
dc.identifier.doi10.1042/BJ20101422-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://dx.doi.org/10.1042/BJ20101422es_ES
dc.identifier.e-issn1470-8728-
dc.contributor.funderMinisterio de Ciencia y Tecnología (España)es_ES
dc.contributor.funderJunta de Andalucíaes_ES
dc.contributor.funderUniversidad Pablo de Olavidees_ES
dc.relation.csices_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100006280es_ES
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