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Dual targeted poplar ferredoxin NADP(+) oxidoreductase interacts with hemoglobin 1.
Journal article

Dual targeted poplar ferredoxin NADP(+) oxidoreductase interacts with hemoglobin 1.

  • Jokipii-Lukkari S Genetics and Physiology Department, University of Oulu, P.O. Box 3000, FI-90014, Finland.
  • Kastaniotis AJ The Faculty of Biochemistry and Molecular Medicine and Biocenter Oulu, University of Oulu, P.O. Box 5400, FI-90014, Finland.
  • Parkash V The Structural Bioinformatics Laboratory, Biochemistry, Faculty of Science and Engineering, Åbo Akademi University, FI-20520 Turku, Finland.
  • Sundström R The Structural Bioinformatics Laboratory, Biochemistry, Faculty of Science and Engineering, Åbo Akademi University, FI-20520 Turku, Finland.
  • Leiva-Eriksson N The Pure and Applied Biochemistry, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden.
  • Nymalm Y The Structural Bioinformatics Laboratory, Biochemistry, Faculty of Science and Engineering, Åbo Akademi University, FI-20520 Turku, Finland.
  • Blokhina O The Department of Biosciences, University of Helsinki, Viikki Biocenter 3, P.O. Box 65, FI-00014, Finland.
  • Kukkola E The Department of Biosciences, University of Helsinki, Viikki Biocenter 3, P.O. Box 65, FI-00014, Finland.
  • Fagerstedt KV The Department of Biosciences, University of Helsinki, Viikki Biocenter 3, P.O. Box 65, FI-00014, Finland.
  • Salminen TA The Structural Bioinformatics Laboratory, Biochemistry, Faculty of Science and Engineering, Åbo Akademi University, FI-20520 Turku, Finland.
  • Läärä E The Department of Mathematical Sciences, University of Oulu, P.O. Box 3000, FI-90014, Finland.
  • Bülow L The Pure and Applied Biochemistry, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden.
  • Ohlmeier S The Faculty of Biochemistry and Molecular Medicine and Biocenter Oulu, University of Oulu, P.O. Box 5400, FI-90014, Finland.
  • Hiltunen JK The Faculty of Biochemistry and Molecular Medicine and Biocenter Oulu, University of Oulu, P.O. Box 5400, FI-90014, Finland.
  • Kallio PT The Institute of Microbiology, ETH-Zürich, CH-8093 Zürich, Switzerland.
  • Häggman H Genetics and Physiology Department, University of Oulu, P.O. Box 3000, FI-90014, Finland. Electronic address: hely.haggman@oulu.fi.
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  • 2016-04-21
Published in:
  • Plant science : an international journal of experimental plant biology. - 2016
Dioxygenation
Dual targeting
Ferredoxin NADP(+) oxidoreductase
Hemoglobin
Nitric oxide
Poplar
Chloroplasts
Cytosol
Ferredoxin-NADP Reductase
Genes, Reporter
Hemoglobins
Mitochondria
Mutation
Nitric Oxide
Oxygenases
Plant Proteins
Populus
Proteomics
Recombinant Fusion Proteins
Saccharomyces cerevisiae
Sequence Analysis, DNA
English Previous reports have connected non-symbiotic and truncated hemoglobins (Hbs) to metabolism of nitric oxide (NO), an important signalling molecule involved in wood formation. We have studied the capability of poplar (Populus tremula × tremuloides) Hbs PttHb1 and PttTrHb proteins alone or with a flavin-protein reductase to relieve NO cytotoxicity in living cells. Complementation tests in a Hb-deficient, NO-sensitive yeast (Saccharomyces cerevisiae) Δyhb1 mutant showed that neither PttHb1 nor PttTrHb alone protected cells against NO. To study the ability of Hbs to interact with a reductase, ferredoxin NADP(+) oxidoreductase PtthFNR was characterized by sequencing and proteomics. To date, by far the greatest number of the known dual-targeted plant proteins are directed to chloroplasts and mitochondria. We discovered a novel variant of hFNR that lacks the plastid presequence and resides in cytosol. The coexpression of PttHb1 and PtthFNR partially restored NO resistance of the yeast Δyhb1 mutant, whereas PttTrHb coexpressed with PtthFNR failed to rescue growth. YFP fusion proteins confirmed the interaction between PttHb1 and PtthFNR in plant cells. The structural modelling results indicate that PttHb1 and PtthFNR are able to interact as NO dioxygenase. This is the first report on dual targeting of central plant enzyme FNR to plastids and cytosol.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://sonar.ch/global/documents/36598
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