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dc.contributor.authorMork-Jansson, Astrid
dc.contributor.authorBue, Ann Kristin
dc.contributor.authorGargano, Daniela
dc.contributor.authorFurnes, Clemens
dc.contributor.authorReisinger, Veronika
dc.contributor.authorArnold, Janine
dc.contributor.authorKmiec, Karol
dc.contributor.authorEichacker, Lutz Andreas
dc.date.accessioned2017-04-12T08:18:33Z
dc.date.available2017-04-12T08:18:33Z
dc.date.issued2015-06
dc.identifier.citationMork-Jansson A. et al. (2015) Lil3 assembles with proteins regulating chlorophyll synthesis in barley. PLoS One, 10(7): e0133145nb_NO
dc.identifier.urihttp://hdl.handle.net/11250/2437498
dc.description.abstractThe light-harvesting-like (LIL) proteins are a family of membrane proteins that share a chlorophyll a/b-binding motif with the major light-harvesting antenna proteins of oxygenic photoautotrophs. LIL proteins have been associated with the regulation of tetrapyrrol biosynthesis, and plant responses to light-stress. Here, it was found in a native PAGE approach that chlorophyllide, and chlorophyllide plus geranylgeraniolpyrophosphate trigger assembly of Lil3 in three chlorine binding fluorescent protein bands, termed F1, F2, and F3. It is shown that light and chlorophyllide trigger accumulation of protochlorophyllide-oxidoreductase, and chlorophyll synthase in band F3. Chlorophyllide and chlorophyll esterified to geranylgeraniol were identified as basis of fluorescence recorded from band F3. A direct interaction between Lil3, CHS and POR was confirmed in a split ubiquitin assay. In the presence of light or chlorophyllide, geranylgeraniolpyrophosphate was shown to trigger a loss of the F3 band and accumulation of Lil3 and geranylgeranyl reductase in F1 and F2. No direct interaction between Lil3 and geranylgeraniolreductase was identified in a split ubiquitin assay; however, accumulation of chlorophyll esterified to phytol in F1 and F2 corroborated the enzymes assembly. Chlorophyll esterified to phytol and the reaction center protein psbD of photosystem II were identified to accumulate together with psb29, and APX in the fluorescent band F2. Data show that Lil3 assembles with proteins regulating chlorophyll synthesis in etioplasts from barley (Hordeum vulgare L.).nb_NO
dc.language.isoengnb_NO
dc.publisherPublic Library of Science (PLoS)nb_NO
dc.rightsNavngivelse 4.0 Internasjonal*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/deed.no*
dc.subjectpigmentsnb_NO
dc.subjectetioplastsnb_NO
dc.subjectfluorescencenb_NO
dc.subjectplastidsnb_NO
dc.subjectprotein complexesnb_NO
dc.subjectbarleynb_NO
dc.subjectchlorophyllnb_NO
dc.titleLil3 assembles with proteins regulating chlorophyll synthesis in barleynb_NO
dc.typeJournal articlenb_NO
dc.typePeer reviewednb_NO
dc.rights.holder© 2015 Mork-Jansson et al.nb_NO
dc.subject.nsiVDP::Matematikk og Naturvitenskap: 400::Basale biofag: 470nb_NO
dc.source.volume10nb_NO
dc.source.journalPLoS Onenb_NO
dc.source.issue7nb_NO
dc.identifier.doi10.1371/journal.pone.0133145
dc.relation.projectNorges forskningsråd: 192436, 197119nb_NO


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