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Evolution, three-dimensional model and localization of truncated hemoglobin PttTrHb of hybrid aspen.

Identifieur interne : 002240 ( Main/Exploration ); précédent : 002239; suivant : 002241

Evolution, three-dimensional model and localization of truncated hemoglobin PttTrHb of hybrid aspen.

Auteurs : Estelle Dumont [France] ; Soile Jokipii-Lukkari [Finlande] ; Vimal Parkash [Finlande] ; Jaana Vuosku [Finlande] ; Robin Sundström [Finlande] ; Yvonne Nymalm [Finlande] ; Suvi Sutela [Finlande] ; Katariina Taskinen [Finlande] ; Pauli T. Kallio [Suisse] ; Tiina A. Salminen [Finlande] ; Hely H Ggman [Finlande]

Source :

RBID : pubmed:24520401

Descripteurs français

English descriptors

Abstract

Thus far, research on plant hemoglobins (Hbs) has mainly concentrated on symbiotic and non-symbiotic Hbs, and information on truncated Hbs (TrHbs) is scarce. The aim of this study was to examine the origin, structure and localization of the truncated Hb (PttTrHb) of hybrid aspen (Populus tremula L. × tremuloides Michx.), the model system of tree biology. Additionally, we studied the PttTrHb expression in relation to non-symbiotic class1 Hb gene (PttHb1) using RNAi-silenced hybrid aspen lines. Both the phylogenetic analysis and the three-dimensional (3D) model of PttTrHb supported the view that plant TrHbs evolved vertically from a bacterial TrHb. The 3D model suggested that PttTrHb adopts a 2-on-2 sandwich of α-helices and has a Bacillus subtilis -like ligand-binding pocket in which E11Gln and B10Tyr form hydrogen bonds to a ligand. However, due to differences in tunnel cavity and gate residue (E7Ala), it might not show similar ligand-binding kinetics as in Bs-HbO (E7Thr). The immunolocalization showed that PttTrHb protein was present in roots, stems as well as leaves of in vitro -grown hybrid aspens. In mature organs, PttTrHb was predominantly found in the vascular bundles and specifically at the site of lateral root formation, overlapping consistently with areas of nitric oxide (NO) production in plants. Furthermore, the NO donor sodium nitroprusside treatment increased the amount of PttTrHb in stems. The observed PttTrHb localization suggests that PttTrHb plays a role in the NO metabolism.

DOI: 10.1371/journal.pone.0088573
PubMed: 24520401
PubMed Central: PMC3919811


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Le document en format XML

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<term>Amino Acid Sequence (MeSH)</term>
<term>Biological Evolution (MeSH)</term>
<term>Gene Expression Regulation, Plant (MeSH)</term>
<term>Heme (chemistry)</term>
<term>Heme (metabolism)</term>
<term>Hybridization, Genetic (MeSH)</term>
<term>Models, Molecular (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Phylogeny (MeSH)</term>
<term>Plant Leaves (metabolism)</term>
<term>Plant Stems (metabolism)</term>
<term>Plants, Genetically Modified (MeSH)</term>
<term>Populus (genetics)</term>
<term>Populus (metabolism)</term>
<term>Protein Transport (MeSH)</term>
<term>RNA Interference (MeSH)</term>
<term>Sequence Alignment (MeSH)</term>
<term>Structural Homology, Protein (MeSH)</term>
<term>Truncated Hemoglobins (chemistry)</term>
<term>Truncated Hemoglobins (genetics)</term>
<term>Truncated Hemoglobins (metabolism)</term>
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<term>Alignement de séquences (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Feuilles de plante (métabolisme)</term>
<term>Hybridation génétique (MeSH)</term>
<term>Hème (composition chimique)</term>
<term>Hème (métabolisme)</term>
<term>Hémoglobines tronquées (composition chimique)</term>
<term>Hémoglobines tronquées (génétique)</term>
<term>Hémoglobines tronquées (métabolisme)</term>
<term>Interférence par ARN (MeSH)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Phylogenèse (MeSH)</term>
<term>Populus (génétique)</term>
<term>Populus (métabolisme)</term>
<term>Régulation de l'expression des gènes végétaux (MeSH)</term>
<term>Similitude structurale de protéines (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Tiges de plante (métabolisme)</term>
<term>Transport des protéines (MeSH)</term>
<term>Végétaux génétiquement modifiés (MeSH)</term>
<term>Évolution biologique (MeSH)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en">
<term>Heme</term>
<term>Truncated Hemoglobins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en">
<term>Truncated Hemoglobins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en">
<term>Heme</term>
<term>Truncated Hemoglobins</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr">
<term>Hème</term>
<term>Hémoglobines tronquées</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en">
<term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr">
<term>Hémoglobines tronquées</term>
<term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en">
<term>Plant Leaves</term>
<term>Plant Stems</term>
<term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr">
<term>Feuilles de plante</term>
<term>Hème</term>
<term>Hémoglobines tronquées</term>
<term>Populus</term>
<term>Tiges de plante</term>
</keywords>
<keywords scheme="MESH" xml:lang="en">
<term>Amino Acid Sequence</term>
<term>Biological Evolution</term>
<term>Gene Expression Regulation, Plant</term>
<term>Hybridization, Genetic</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Phylogeny</term>
<term>Plants, Genetically Modified</term>
<term>Protein Transport</term>
<term>RNA Interference</term>
<term>Sequence Alignment</term>
<term>Structural Homology, Protein</term>
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<term>Alignement de séquences</term>
<term>Données de séquences moléculaires</term>
<term>Hybridation génétique</term>
<term>Interférence par ARN</term>
<term>Modèles moléculaires</term>
<term>Phylogenèse</term>
<term>Régulation de l'expression des gènes végétaux</term>
<term>Similitude structurale de protéines</term>
<term>Séquence d'acides aminés</term>
<term>Transport des protéines</term>
<term>Végétaux génétiquement modifiés</term>
<term>Évolution biologique</term>
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<div type="abstract" xml:lang="en">Thus far, research on plant hemoglobins (Hbs) has mainly concentrated on symbiotic and non-symbiotic Hbs, and information on truncated Hbs (TrHbs) is scarce. The aim of this study was to examine the origin, structure and localization of the truncated Hb (PttTrHb) of hybrid aspen (Populus tremula L. × tremuloides Michx.), the model system of tree biology. Additionally, we studied the PttTrHb expression in relation to non-symbiotic class1 Hb gene (PttHb1) using RNAi-silenced hybrid aspen lines. Both the phylogenetic analysis and the three-dimensional (3D) model of PttTrHb supported the view that plant TrHbs evolved vertically from a bacterial TrHb. The 3D model suggested that PttTrHb adopts a 2-on-2 sandwich of α-helices and has a Bacillus subtilis -like ligand-binding pocket in which E11Gln and B10Tyr form hydrogen bonds to a ligand. However, due to differences in tunnel cavity and gate residue (E7Ala), it might not show similar ligand-binding kinetics as in Bs-HbO (E7Thr). The immunolocalization showed that PttTrHb protein was present in roots, stems as well as leaves of in vitro -grown hybrid aspens. In mature organs, PttTrHb was predominantly found in the vascular bundles and specifically at the site of lateral root formation, overlapping consistently with areas of nitric oxide (NO) production in plants. Furthermore, the NO donor sodium nitroprusside treatment increased the amount of PttTrHb in stems. The observed PttTrHb localization suggests that PttTrHb plays a role in the NO metabolism. </div>
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<AbstractText>Thus far, research on plant hemoglobins (Hbs) has mainly concentrated on symbiotic and non-symbiotic Hbs, and information on truncated Hbs (TrHbs) is scarce. The aim of this study was to examine the origin, structure and localization of the truncated Hb (PttTrHb) of hybrid aspen (Populus tremula L. × tremuloides Michx.), the model system of tree biology. Additionally, we studied the PttTrHb expression in relation to non-symbiotic class1 Hb gene (PttHb1) using RNAi-silenced hybrid aspen lines. Both the phylogenetic analysis and the three-dimensional (3D) model of PttTrHb supported the view that plant TrHbs evolved vertically from a bacterial TrHb. The 3D model suggested that PttTrHb adopts a 2-on-2 sandwich of α-helices and has a Bacillus subtilis -like ligand-binding pocket in which E11Gln and B10Tyr form hydrogen bonds to a ligand. However, due to differences in tunnel cavity and gate residue (E7Ala), it might not show similar ligand-binding kinetics as in Bs-HbO (E7Thr). The immunolocalization showed that PttTrHb protein was present in roots, stems as well as leaves of in vitro -grown hybrid aspens. In mature organs, PttTrHb was predominantly found in the vascular bundles and specifically at the site of lateral root formation, overlapping consistently with areas of nitric oxide (NO) production in plants. Furthermore, the NO donor sodium nitroprusside treatment increased the amount of PttTrHb in stems. The observed PttTrHb localization suggests that PttTrHb plays a role in the NO metabolism. </AbstractText>
</Abstract>
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<Author ValidYN="Y">
<LastName>Dumont</LastName>
<ForeName>Estelle</ForeName>
<Initials>E</Initials>
<AffiliationInfo>
<Affiliation>Department of Biology, University of Oulu, Oulu, Finland ; UMR-MD1, Transporteurs Membranaires, Chimiorésistance et Drug-Design, Aix-Marseille Université, Marseille, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Jokipii-Lukkari</LastName>
<ForeName>Soile</ForeName>
<Initials>S</Initials>
<AffiliationInfo>
<Affiliation>Department of Biology, University of Oulu, Oulu, Finland.</Affiliation>
</AffiliationInfo>
</Author>
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<LastName>Parkash</LastName>
<ForeName>Vimal</ForeName>
<Initials>V</Initials>
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<Affiliation>Structural Bioinformatics Laboratory, Department of Biosciences, Åbo Akademi University, Turku, Finland.</Affiliation>
</AffiliationInfo>
</Author>
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<LastName>Vuosku</LastName>
<ForeName>Jaana</ForeName>
<Initials>J</Initials>
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<Affiliation>Department of Biology, University of Oulu, Oulu, Finland.</Affiliation>
</AffiliationInfo>
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<LastName>Sundström</LastName>
<ForeName>Robin</ForeName>
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<Affiliation>Structural Bioinformatics Laboratory, Department of Biosciences, Åbo Akademi University, Turku, Finland.</Affiliation>
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<LastName>Nymalm</LastName>
<ForeName>Yvonne</ForeName>
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<Affiliation>Structural Bioinformatics Laboratory, Department of Biosciences, Åbo Akademi University, Turku, Finland.</Affiliation>
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<LastName>Sutela</LastName>
<ForeName>Suvi</ForeName>
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<Affiliation>Department of Biology, University of Oulu, Oulu, Finland.</Affiliation>
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</AffiliationInfo>
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<LastName>Salminen</LastName>
<ForeName>Tiina A</ForeName>
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<Author ValidYN="Y">
<LastName>Häggman</LastName>
<ForeName>Hely</ForeName>
<Initials>H</Initials>
<AffiliationInfo>
<Affiliation>Department of Biology, University of Oulu, Oulu, Finland.</Affiliation>
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   |texte=   Evolution, three-dimensional model and localization of truncated hemoglobin PttTrHb of hybrid aspen.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i   -Sk "pubmed:24520401" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd   \
       | NlmPubMed2Wicri -a PoplarV1 

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