Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/28894
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dc.contributor.authorYruela Guerrero, Inmaculada-
dc.contributor.authorArilla-Luna, Sonia-
dc.contributor.authorMedina, Milagros-
dc.contributor.authorContreras-Moreira, Bruno-
dc.date.accessioned2010-11-04T08:40:20Z-
dc.date.available2010-11-04T08:40:20Z-
dc.date.issued2010-10-
dc.identifier.citationYruela I, Arilla-Luna S, Medina M. Evolutionary divergence of chloroplast FAD synthetase proteins. BMC Evolutionary Biology 10: 311 (2010)es_ES
dc.identifier.issn1471-2148-
dc.identifier.urihttp://hdl.handle.net/10261/28894-
dc.description13 Pag., 2 Tabl., 4 Fig.es_ES
dc.description.abstractBackground Flavin adenine dinucleotide synthetases (FADSs) - a group of bifunctional enzymes that carry out the dual functions of riboflavin phosphorylation to produce flavin mononucleotide (FMN) and its subsequent adenylation to generate FAD in most prokaryotes - were studied in plants in terms of sequence, structure and evolutionary history. Results Using a variety of bioinformatics methods we have found that FADS enzymes localized to the chloroplasts, which we term as plant-like FADS proteins, are distributed across a variety of green plant lineages and constitute a divergent protein family clearly of cyanobacterial origin. The C-terminal module of these enzymes does not contain the typical riboflavin kinase active site sequence, while the N-terminal module is broadly conserved. These results agree with a previous work reported by Sandoval et al. in 2008. Furthermore, our observations and preliminary experimental results indicate that the C-terminus of plant-like FADS proteins may contain a catalytic activity, but different to that of their prokaryotic counterparts. In fact, homology models predict that plant-specific conserved residues constitute a distinct active site in the C-terminus. Conclusions A structure-based sequence alignment and an in-depth evolutionary survey of FADS proteins, thought to be crucial in plant metabolism, are reported, which will be essential for the correct annotation of plant genomes and further structural and functional studies. This work is a contribution to our understanding of the evolutionary history of plant-like FADS enzymes, which constitute a new family of FADS proteins whose C-terminal module might be involved in a distinct catalytic activity.es_ES
dc.description.sponsorshipThis work was supported by CONSI+D, DGA (Grant PM062/2007 to M.M. and I.Y.), the Spanish Ministry of Science and Innovation (BIO2007-65890-C02-01 and BIO2010-14983 to M.M.) and Gobierno de Aragón (DGA-GE B18 to M. M. and I.Y. and DGA-GC A06 to B.C-M).es_ES
dc.language.isoenges_ES
dc.publisherBioMed Centrales_ES
dc.relation.isversionofPublisher’s version-
dc.rightsopenAccesses_ES
dc.titleEvolutionary divergence of chloroplast FAD synthetase proteinses_ES
dc.typeartículoes_ES
dc.identifier.doi10.1186/1471-2148-10-311-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://dx.doi.org/10.1186/1471-2148-10-311es_ES
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item.cerifentitytypePublications-
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.grantfulltextopen-
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