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dc.contributor.authorRaynaud, Sandyes_ES
dc.contributor.authorRagel, Paulaes_ES
dc.contributor.authorMérida, Ángeles_ES
dc.date.accessioned2016-05-30T09:30:21Z-
dc.date.available2016-05-30T09:30:21Z-
dc.date.issued2016-
dc.identifier.citationJournal of Biological Chemistry, 291(20): 10759-107771 (2016)es_ES
dc.identifier.urihttp://hdl.handle.net/10261/132738-
dc.description.abstractStarch synthase 4 (SS4) plays a specific role in starch synthesis because it controls the number of starch granules synthesized in the chloroplast and is involved in the initiation of the starch granule. We showed previously that SS4 interacts with fibrillins 1 and is associated with plastoglobules, suborganelle compartments physically attached to the thylakoid membrane in chloroplasts. Both SS4 localization and its interaction with fibrillins 1 were mediated by the N-terminal part of SS4. Here we show that the coiled-coil region within the N-terminal portion of SS4 is involved in both processes. Elimination of this region prevents SS4 from binding to fibrillins 1 and alters SS4 localization in the chloroplast. We also show that SS4 forms dimers, which depends on a region located between the coiled-coil region and the glycosyltransferase domain of SS4. This region is highly conserved between all SS4 enzymes sequenced to date.Weshow that the dimerization seems to be necessary for the activity of the enzyme. Both dimerization and the functionality of the coiled-coil region are conserved among SS4 proteins from phylogenetically distant species, such as Arabidopsis and Brachypodium. This finding suggests that the mechanism of action of SS4 is conserved among different plant species.es_ES
dc.language.isoenges_ES
dc.publisherAmerican Society for Biochemistry and Molecular Biologyes_ES
dc.relation.isversionofPublisher's versiones_ES
dc.rightsopenAccessen_EN
dc.titleThe N-terminal Part of Arabidopsis thaliana Starch Synthase 4 Determines the Localization and Activity of the Enzymees_ES
dc.typeartículoes_ES
dc.identifier.doi10.1074/jbc.M115.698332-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://dx.doi.org/10.1074/jbc.M115.698332es_ES
dc.embargo.terms2017-05-14es_ES
dc.relation.csices_ES
oprm.item.hasRevisionno ko 0 false*
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