title: Cyanobacterial flavodoxin complements ferredoxin deficiency in knocked-down transgenic tobacco plants.
abstract: Ferredoxins are the main electron shuttles in chloroplasts, accepting electrons from photosystem I and delivering them to essential oxido-reductive pathways in the stroma. Ferredoxin levels decrease under adverse environmental conditions in both plants and photosynthetic micro-organisms. In cyanobacteria and some algae, this decrease is compensated for by induction of flavodoxin, an isofunctional flavoprotein that can replace ferredoxin in many reactions. Flavodoxin is not present in plants, but tobacco lines expressing a plastid-targeted cyanobacterial flavodoxin developed increased tolerance to environmental stress. Chloroplast-located flavodoxin interacts productively with endogenous ferredoxin-dependent pathways, suggesting that its protective role results from replacement of stress-labile ferredoxin. We tested this hypothesis by using RNA antisense and interference techniques to decrease ferredoxin levels in transgenic tobacco. Ferredoxin-deficient lines showed growth arrest, leaf chlorosis and decreased CO(2) assimilation. Chlorophyll fluorescence measurements indicated impaired photochemistry, over-reduction of the photosynthetic electron transport chain and enhanced non-photochemical quenching. Expression of flavodoxin from the nuclear or plastid genome restored growth, pigment contents and photosynthetic capacity, and relieved the electron pressure on the electron transport chain. Tolerance to oxidative stress also recovered. In the absence of flavodoxin, ferredoxin could not be decreased below 45% of physiological content without fatally compromising plant survival, but in its presence, lines with only 12% remaining ferredoxin could grow autotrophically, with almost wild-type phenotypes. The results indicate that the stress tolerance conferred by flavodoxin expression in plants stems largely from functional complementation of endogenous ferredoxin by the cyanobacterial flavoprotein.
authors.affiliation: División Biología Molecular, Facultad de Ciencias Bioquímicas y Farmacéuticas, Instituto de Biología Molecular y Celular de Rosario (IBR, CONICET), Universidad Nacional de Rosario, S2002LRK Rosario, Argentina.
authors.forename: Nicolás E
authors.initials: NE
authors.lastname: Blanco
authors.forename: Romina D
authors.initials: RD
authors.lastname: Ceccoli
authors.forename: María E
authors.initials: ME
authors.lastname: Segretin
authors.forename: Hugo O
authors.initials: HO
authors.lastname: Poli
authors.forename: Ingo
authors.initials: I
authors.lastname: Voss
authors.forename: Michael
authors.initials: M
authors.lastname: Melzer
authors.forename: Fernando F
authors.initials: FF
authors.lastname: Bravo-Almonacid
authors.forename: Renate
authors.initials: R
authors.lastname: Scheibe
authors.forename: Mohammad-Reza
authors.initials: MR
authors.lastname: Hajirezaei
authors.forename: Néstor
authors.initials: N
authors.lastname: Carrillo
mesh_terms: D017033:Anabaena / Q000235:genetics / Q000378:metabolism; D001483:Base Sequence; D018744:DNA, Plant / Q000235:genetics; D005288:Ferredoxins / Q000172:deficiency / Q000235:genetics / Q000378:metabolism*; D005418:Flavodoxin / Q000235:genetics* / Q000378:metabolism*; D055785:Gene Knockdown Techniques; D005816:Genetic Complementation Test; D046529:Microscopy, Electron, Transmission; D018515:Plant Leaves / Q000378:metabolism / Q000648:ultrastructure; D030821:Plants, Genetically Modified; D034622:RNA Interference; D016372:RNA, Antisense / Q000235:genetics; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D013312:Stress, Physiological; D014026:Nicotiana / Q000235:genetics* / Q000378:metabolism* / Q000648:ultrastructure
chemical_list: D018744:DNA, Plant; D005288:Ferredoxins; D005418:Flavodoxin; D016372:RNA, Antisense; D011994:Recombinant Proteins