PoplarV1, Main, Exploration, bibRecord, 001912

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

Identifieur interne : 001912 ( Main/Exploration ); précédent : 001911; suivant : 001913

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

Auteurs : Soile Jokipii-Lukkari [Finlande] ; Alexander J. Kastaniotis [Finlande] ; Vimal Parkash [Finlande] ; Robin Sundström [Finlande] ; Nélida Leiva-Eriksson [Suède] ; Yvonne Nymalm [Finlande] ; Olga Blokhina [Finlande] ; Eija Kukkola [Finlande] ; Kurt V. Fagerstedt [Finlande] ; Tiina A. Salminen [Finlande] ; Esa L R [Finlande] ; Leif Bülow [Suède] ; Steffen Ohlmeier [Finlande] ; J Kalervo Hiltunen [Finlande] ; Pauli T. Kallio [Suisse] ; Hely H Ggman [Finlande]

Source :

Plant science : an international journal of experimental plant biology [ 1873-2259 ] ; 2016.

RBID : pubmed:27095407

Descripteurs français

KwdFr :
- Analyse de séquence d'ADN (MeSH), Chloroplastes (métabolisme), Cytosol (métabolisme), Ferredoxine-NADP reductase (génétique), Ferredoxine-NADP reductase (métabolisme), Gènes rapporteurs (MeSH), Hémoglobines (métabolisme), Mitochondries (métabolisme), Monoxyde d'azote (pharmacologie), Mutation (MeSH), Oxygénases (génétique), Oxygénases (métabolisme), Populus (enzymologie), Populus (génétique), Protéines de fusion recombinantes (MeSH), Protéines végétales (génétique), Protéines végétales (métabolisme), Protéomique (MeSH), Saccharomyces cerevisiae (effets des médicaments et des substances chimiques), Saccharomyces cerevisiae (enzymologie), Saccharomyces cerevisiae (génétique).
MESH :
- effets des médicaments et des substances chimiques : Saccharomyces cerevisiae.
- enzymologie : Populus, Saccharomyces cerevisiae.
- génétique : Ferredoxine-NADP reductase, Oxygénases, Populus, Protéines végétales, Saccharomyces cerevisiae.
- métabolisme : Chloroplastes, Cytosol, Ferredoxine-NADP reductase, Hémoglobines, Mitochondries, Oxygénases, Protéines végétales.
- pharmacologie : Monoxyde d'azote.
- Analyse de séquence d'ADN, Gènes rapporteurs, Mutation, Protéines de fusion recombinantes, Protéomique.

English descriptors

KwdEn :
- Chloroplasts (metabolism), Cytosol (metabolism), Ferredoxin-NADP Reductase (genetics), Ferredoxin-NADP Reductase (metabolism), Genes, Reporter (MeSH), Hemoglobins (metabolism), Mitochondria (metabolism), Mutation (MeSH), Nitric Oxide (pharmacology), Oxygenases (genetics), Oxygenases (metabolism), Plant Proteins (genetics), Plant Proteins (metabolism), Populus (enzymology), Populus (genetics), Proteomics (MeSH), Recombinant Fusion Proteins (MeSH), Saccharomyces cerevisiae (drug effects), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae (genetics), Sequence Analysis, DNA (MeSH).
MESH :
- chemical , genetics : Ferredoxin-NADP Reductase, Oxygenases, Plant Proteins.
- drug effects : Saccharomyces cerevisiae.
- enzymology : Populus, Saccharomyces cerevisiae.
- genetics : Populus, Saccharomyces cerevisiae.
- metabolism : Chloroplasts, Cytosol, Ferredoxin-NADP Reductase, Hemoglobins, Mitochondria, Oxygenases, Plant Proteins.
- chemical , pharmacology : Nitric Oxide.
- Genes, Reporter, Mutation, Proteomics, Recombinant Fusion Proteins, Sequence Analysis, DNA.

Abstract

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.

DOI: 10.1016/j.plantsci.2016.03.013
PubMed: 27095407

Affiliations:

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Le document en format XML

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<author><name sortKey="Hiltunen, J Kalervo" sort="Hiltunen, J Kalervo" uniqKey="Hiltunen J" first="J Kalervo" last="Hiltunen">J Kalervo Hiltunen</name>
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<author><name sortKey="Kallio, Pauli T" sort="Kallio, Pauli T" uniqKey="Kallio P" first="Pauli T" last="Kallio">Pauli T. Kallio</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Dual targeted poplar ferredoxin NADP(+) oxidoreductase interacts with hemoglobin 1.</title>
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<author><name sortKey="Kastaniotis, Alexander J" sort="Kastaniotis, Alexander J" uniqKey="Kastaniotis A" first="Alexander J" last="Kastaniotis">Alexander J. Kastaniotis</name>
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<country xml:lang="fr">Finlande</country>
<wicri:regionArea>The Faculty of Biochemistry and Molecular Medicine and Biocenter Oulu, University of Oulu, P.O. Box 5400, FI-90014</wicri:regionArea>
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<author><name sortKey="Parkash, Vimal" sort="Parkash, Vimal" uniqKey="Parkash V" first="Vimal" last="Parkash">Vimal Parkash</name>
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<author><name sortKey="Sundstrom, Robin" sort="Sundstrom, Robin" uniqKey="Sundstrom R" first="Robin" last="Sundström">Robin Sundström</name>
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<author><name sortKey="Leiva Eriksson, Nelida" sort="Leiva Eriksson, Nelida" uniqKey="Leiva Eriksson N" first="Nélida" last="Leiva-Eriksson">Nélida Leiva-Eriksson</name>
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<country xml:lang="fr">Suède</country>
<wicri:regionArea>The Pure and Applied Biochemistry, Lund University, P.O. Box 124, SE-221 00 Lund</wicri:regionArea>
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<author><name sortKey="Nymalm, Yvonne" sort="Nymalm, Yvonne" uniqKey="Nymalm Y" first="Yvonne" last="Nymalm">Yvonne Nymalm</name>
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<author><name sortKey="Fagerstedt, Kurt V" sort="Fagerstedt, Kurt V" uniqKey="Fagerstedt K" first="Kurt V" last="Fagerstedt">Kurt V. Fagerstedt</name>
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<country xml:lang="fr">Finlande</country>
<wicri:regionArea>The Department of Biosciences, University of Helsinki, Viikki Biocenter 3, P.O. Box 65, FI-00014</wicri:regionArea>
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<author><name sortKey="Salminen, Tiina A" sort="Salminen, Tiina A" uniqKey="Salminen T" first="Tiina A" last="Salminen">Tiina A. Salminen</name>
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<author><name sortKey="L R, Esa" sort="L R, Esa" uniqKey="L R E" first="Esa" last="L R">Esa L R</name>
<affiliation wicri:level="1"><nlm:affiliation>The Department of Mathematical Sciences, University of Oulu, P.O. Box 3000, FI-90014, Finland.</nlm:affiliation>
<country xml:lang="fr">Finlande</country>
<wicri:regionArea>The Department of Mathematical Sciences, University of Oulu, P.O. Box 3000, FI-90014</wicri:regionArea>
<wicri:noRegion>FI-90014</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Bulow, Leif" sort="Bulow, Leif" uniqKey="Bulow L" first="Leif" last="Bülow">Leif Bülow</name>
<affiliation wicri:level="1"><nlm:affiliation>The Pure and Applied Biochemistry, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden.</nlm:affiliation>
<country xml:lang="fr">Suède</country>
<wicri:regionArea>The Pure and Applied Biochemistry, Lund University, P.O. Box 124, SE-221 00 Lund</wicri:regionArea>
<wicri:noRegion>SE-221 00 Lund</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Ohlmeier, Steffen" sort="Ohlmeier, Steffen" uniqKey="Ohlmeier S" first="Steffen" last="Ohlmeier">Steffen Ohlmeier</name>
<affiliation wicri:level="1"><nlm:affiliation>The Faculty of Biochemistry and Molecular Medicine and Biocenter Oulu, University of Oulu, P.O. Box 5400, FI-90014, Finland.</nlm:affiliation>
<country xml:lang="fr">Finlande</country>
<wicri:regionArea>The Faculty of Biochemistry and Molecular Medicine and Biocenter Oulu, University of Oulu, P.O. Box 5400, FI-90014</wicri:regionArea>
<wicri:noRegion>FI-90014</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Hiltunen, J Kalervo" sort="Hiltunen, J Kalervo" uniqKey="Hiltunen J" first="J Kalervo" last="Hiltunen">J Kalervo Hiltunen</name>
<affiliation wicri:level="1"><nlm:affiliation>The Faculty of Biochemistry and Molecular Medicine and Biocenter Oulu, University of Oulu, P.O. Box 5400, FI-90014, Finland.</nlm:affiliation>
<country xml:lang="fr">Finlande</country>
<wicri:regionArea>The Faculty of Biochemistry and Molecular Medicine and Biocenter Oulu, University of Oulu, P.O. Box 5400, FI-90014</wicri:regionArea>
<wicri:noRegion>FI-90014</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Kallio, Pauli T" sort="Kallio, Pauli T" uniqKey="Kallio P" first="Pauli T" last="Kallio">Pauli T. Kallio</name>
<affiliation wicri:level="1"><nlm:affiliation>The Institute of Microbiology, ETH-Zürich, CH-8093 Zürich, Switzerland.</nlm:affiliation>
<country xml:lang="fr">Suisse</country>
<wicri:regionArea>The Institute of Microbiology, ETH-Zürich, CH-8093 Zürich</wicri:regionArea>
<wicri:noRegion>CH-8093 Zürich</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="H Ggman, Hely" sort="H Ggman, Hely" uniqKey="H Ggman H" first="Hely" last="H Ggman">Hely H Ggman</name>
<affiliation wicri:level="1"><nlm:affiliation>Genetics and Physiology Department, University of Oulu, P.O. Box 3000, FI-90014, Finland. Electronic address: hely.haggman@oulu.fi.</nlm:affiliation>
<country xml:lang="fr">Finlande</country>
<wicri:regionArea>Genetics and Physiology Department, University of Oulu, P.O. Box 3000, FI-90014</wicri:regionArea>
<wicri:noRegion>FI-90014</wicri:noRegion>
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</author>
</analytic>
<series><title level="j">Plant science : an international journal of experimental plant biology</title>
<idno type="eISSN">1873-2259</idno>
<imprint><date when="2016" type="published">2016</date>
</imprint>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Chloroplasts (metabolism)</term>
<term>Cytosol (metabolism)</term>
<term>Ferredoxin-NADP Reductase (genetics)</term>
<term>Ferredoxin-NADP Reductase (metabolism)</term>
<term>Genes, Reporter (MeSH)</term>
<term>Hemoglobins (metabolism)</term>
<term>Mitochondria (metabolism)</term>
<term>Mutation (MeSH)</term>
<term>Nitric Oxide (pharmacology)</term>
<term>Oxygenases (genetics)</term>
<term>Oxygenases (metabolism)</term>
<term>Plant Proteins (genetics)</term>
<term>Plant Proteins (metabolism)</term>
<term>Populus (enzymology)</term>
<term>Populus (genetics)</term>
<term>Proteomics (MeSH)</term>
<term>Recombinant Fusion Proteins (MeSH)</term>
<term>Saccharomyces cerevisiae (drug effects)</term>
<term>Saccharomyces cerevisiae (enzymology)</term>
<term>Saccharomyces cerevisiae (genetics)</term>
<term>Sequence Analysis, DNA (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Analyse de séquence d'ADN (MeSH)</term>
<term>Chloroplastes (métabolisme)</term>
<term>Cytosol (métabolisme)</term>
<term>Ferredoxine-NADP reductase (génétique)</term>
<term>Ferredoxine-NADP reductase (métabolisme)</term>
<term>Gènes rapporteurs (MeSH)</term>
<term>Hémoglobines (métabolisme)</term>
<term>Mitochondries (métabolisme)</term>
<term>Monoxyde d'azote (pharmacologie)</term>
<term>Mutation (MeSH)</term>
<term>Oxygénases (génétique)</term>
<term>Oxygénases (métabolisme)</term>
<term>Populus (enzymologie)</term>
<term>Populus (génétique)</term>
<term>Protéines de fusion recombinantes (MeSH)</term>
<term>Protéines végétales (génétique)</term>
<term>Protéines végétales (métabolisme)</term>
<term>Protéomique (MeSH)</term>
<term>Saccharomyces cerevisiae (effets des médicaments et des substances chimiques)</term>
<term>Saccharomyces cerevisiae (enzymologie)</term>
<term>Saccharomyces cerevisiae (génétique)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Ferredoxin-NADP Reductase</term>
<term>Oxygenases</term>
<term>Plant Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Populus</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Populus</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Populus</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Ferredoxine-NADP reductase</term>
<term>Oxygénases</term>
<term>Populus</term>
<term>Protéines végétales</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Chloroplasts</term>
<term>Cytosol</term>
<term>Ferredoxin-NADP Reductase</term>
<term>Hemoglobins</term>
<term>Mitochondria</term>
<term>Oxygenases</term>
<term>Plant Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Chloroplastes</term>
<term>Cytosol</term>
<term>Ferredoxine-NADP reductase</term>
<term>Hémoglobines</term>
<term>Mitochondries</term>
<term>Oxygénases</term>
<term>Protéines végétales</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Monoxyde d'azote</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Nitric Oxide</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Genes, Reporter</term>
<term>Mutation</term>
<term>Proteomics</term>
<term>Recombinant Fusion Proteins</term>
<term>Sequence Analysis, DNA</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Analyse de séquence d'ADN</term>
<term>Gènes rapporteurs</term>
<term>Mutation</term>
<term>Protéines de fusion recombinantes</term>
<term>Protéomique</term>
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<front><div type="abstract" xml:lang="en">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.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27095407</PMID>
<DateCompleted><Year>2016</Year>
<Month>12</Month>
<Day>14</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>09</Month>
<Day>30</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-2259</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>247</Volume>
<PubDate><Year>2016</Year>
<Month>Jun</Month>
</PubDate>
</JournalIssue>
<Title>Plant science : an international journal of experimental plant biology</Title>
<ISOAbbreviation>Plant Sci</ISOAbbreviation>
</Journal>
<ArticleTitle>Dual targeted poplar ferredoxin NADP(+) oxidoreductase interacts with hemoglobin 1.</ArticleTitle>
<Pagination><MedlinePgn>138-49</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1016/j.plantsci.2016.03.013</ELocationID>
<ELocationID EIdType="pii" ValidYN="Y">S0168-9452(16)30044-9</ELocationID>
<Abstract><AbstractText>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.</AbstractText>
<CopyrightInformation>Copyright © 2016 Elsevier Ireland Ltd. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Jokipii-Lukkari</LastName>
<ForeName>Soile</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Genetics and Physiology Department, University of Oulu, P.O. Box 3000, FI-90014, Finland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Kastaniotis</LastName>
<ForeName>Alexander J</ForeName>
<Initials>AJ</Initials>
<AffiliationInfo><Affiliation>The Faculty of Biochemistry and Molecular Medicine and Biocenter Oulu, University of Oulu, P.O. Box 5400, FI-90014, Finland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Parkash</LastName>
<ForeName>Vimal</ForeName>
<Initials>V</Initials>
<AffiliationInfo><Affiliation>The Structural Bioinformatics Laboratory, Biochemistry, Faculty of Science and Engineering, Åbo Akademi University, FI-20520 Turku, Finland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Sundström</LastName>
<ForeName>Robin</ForeName>
<Initials>R</Initials>
<AffiliationInfo><Affiliation>The Structural Bioinformatics Laboratory, Biochemistry, Faculty of Science and Engineering, Åbo Akademi University, FI-20520 Turku, Finland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Leiva-Eriksson</LastName>
<ForeName>Nélida</ForeName>
<Initials>N</Initials>
<AffiliationInfo><Affiliation>The Pure and Applied Biochemistry, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Nymalm</LastName>
<ForeName>Yvonne</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>The Structural Bioinformatics Laboratory, Biochemistry, Faculty of Science and Engineering, Åbo Akademi University, FI-20520 Turku, Finland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Blokhina</LastName>
<ForeName>Olga</ForeName>
<Initials>O</Initials>
<AffiliationInfo><Affiliation>The Department of Biosciences, University of Helsinki, Viikki Biocenter 3, P.O. Box 65, FI-00014, Finland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Kukkola</LastName>
<ForeName>Eija</ForeName>
<Initials>E</Initials>
<AffiliationInfo><Affiliation>The Department of Biosciences, University of Helsinki, Viikki Biocenter 3, P.O. Box 65, FI-00014, Finland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Fagerstedt</LastName>
<ForeName>Kurt V</ForeName>
<Initials>KV</Initials>
<AffiliationInfo><Affiliation>The Department of Biosciences, University of Helsinki, Viikki Biocenter 3, P.O. Box 65, FI-00014, Finland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Salminen</LastName>
<ForeName>Tiina A</ForeName>
<Initials>TA</Initials>
<AffiliationInfo><Affiliation>The Structural Bioinformatics Laboratory, Biochemistry, Faculty of Science and Engineering, Åbo Akademi University, FI-20520 Turku, Finland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Läärä</LastName>
<ForeName>Esa</ForeName>
<Initials>E</Initials>
<AffiliationInfo><Affiliation>The Department of Mathematical Sciences, University of Oulu, P.O. Box 3000, FI-90014, Finland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Bülow</LastName>
<ForeName>Leif</ForeName>
<Initials>L</Initials>
<AffiliationInfo><Affiliation>The Pure and Applied Biochemistry, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Ohlmeier</LastName>
<ForeName>Steffen</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>The Faculty of Biochemistry and Molecular Medicine and Biocenter Oulu, University of Oulu, P.O. Box 5400, FI-90014, Finland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Hiltunen</LastName>
<ForeName>J Kalervo</ForeName>
<Initials>JK</Initials>
<AffiliationInfo><Affiliation>The Faculty of Biochemistry and Molecular Medicine and Biocenter Oulu, University of Oulu, P.O. Box 5400, FI-90014, Finland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Kallio</LastName>
<ForeName>Pauli T</ForeName>
<Initials>PT</Initials>
<AffiliationInfo><Affiliation>The Institute of Microbiology, ETH-Zürich, CH-8093 Zürich, Switzerland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Häggman</LastName>
<ForeName>Hely</ForeName>
<Initials>H</Initials>
<AffiliationInfo><Affiliation>Genetics and Physiology Department, University of Oulu, P.O. Box 3000, FI-90014, Finland. Electronic address: hely.haggman@oulu.fi.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2016</Year>
<Month>03</Month>
<Day>26</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>Ireland</Country>
<MedlineTA>Plant Sci</MedlineTA>
<NlmUniqueID>9882015</NlmUniqueID>
<ISSNLinking>0168-9452</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D006454">Hemoglobins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011993">Recombinant Fusion Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>31C4KY9ESH</RegistryNumber>
<NameOfSubstance UI="D009569">Nitric Oxide</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 1.13.-</RegistryNumber>
<NameOfSubstance UI="D010105">Oxygenases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 1.14.13.-</RegistryNumber>
<NameOfSubstance UI="C114415">nitric oxide dioxygenase</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 1.18.1.2</RegistryNumber>
<NameOfSubstance UI="D005287">Ferredoxin-NADP Reductase</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D002736" MajorTopicYN="N">Chloroplasts</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003600" MajorTopicYN="N">Cytosol</DescriptorName>
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<MeshHeading><DescriptorName UI="D005287" MajorTopicYN="N">Ferredoxin-NADP Reductase</DescriptorName>
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<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
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</MeshHeading>
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<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D040901" MajorTopicYN="N">Proteomics</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011993" MajorTopicYN="N">Recombinant Fusion Proteins</DescriptorName>
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<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
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<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
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<MeshHeading><DescriptorName UI="D017422" MajorTopicYN="N">Sequence Analysis, DNA</DescriptorName>
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<Keyword MajorTopicYN="N">Dual targeting</Keyword>
<Keyword MajorTopicYN="N">Ferredoxin NADP(+) oxidoreductase</Keyword>
<Keyword MajorTopicYN="N">Hemoglobin</Keyword>
<Keyword MajorTopicYN="N">Nitric oxide</Keyword>
<Keyword MajorTopicYN="N">Poplar</Keyword>
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<Month>01</Month>
<Day>07</Day>
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<Month>03</Month>
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<li>Suède</li>
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</region>
<settlement><li>Helsinki</li>
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   |clé=     pubmed:27095407
   |texte=   Dual targeted poplar ferredoxin NADP(+) oxidoreductase interacts with hemoglobin 1.
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Dual targeted poplar ferredoxin NADP(+) oxidoreductase interacts with hemoglobin 1.

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

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