Characterization of histidine-aspartate kinase HK1 and identification of histidine phosphotransfer proteins as potential partners in a Populus multistep phosphorelay.
Identifieur interne : 002727 ( Main/Corpus ); précédent : 002726; suivant : 002728Characterization of histidine-aspartate kinase HK1 and identification of histidine phosphotransfer proteins as potential partners in a Populus multistep phosphorelay.
Auteurs : François Héricourt ; Françoise Chefdor ; Lucie Bertheau ; Mirai Tanigawa ; Tatsuya Maeda ; Grégory Guirimand ; Vincent Courdavault ; Mélanie Larcher ; Christiane Depierreux ; Hélène Bénédetti ; Domenico Morabito ; Franck Brignolas ; Sabine CarpinSource :
- Physiologia plantarum [ 1399-3054 ] ; 2013.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Aspartate Kinase (chemistry), Aspartate Kinase (genetics), Aspartate Kinase (metabolism), Blotting, Western (MeSH), Genetic Complementation Test (MeSH), Histidine (genetics), Histidine (metabolism), Histidine Kinase (MeSH), Intracellular Signaling Peptides and Proteins (genetics), Intracellular Signaling Peptides and Proteins (metabolism), Membrane Proteins (genetics), Membrane Proteins (metabolism), Molecular Sequence Data (MeSH), Mutation (MeSH), Phosphorylation (MeSH), Plant Proteins (chemistry), Plant Proteins (genetics), Plant Proteins (metabolism), Populus (genetics), Populus (metabolism), Protein Binding (MeSH), Protein Kinases (chemistry), Protein Kinases (genetics), Protein Kinases (metabolism), Protein Multimerization (MeSH), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (growth & development), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Sequence Homology, Amino Acid (MeSH), Two-Hybrid System Techniques (MeSH).
- MESH :
- chemical , chemistry : Aspartate Kinase, Plant Proteins, Protein Kinases.
- chemical , genetics : Aspartate Kinase, Histidine, Intracellular Signaling Peptides and Proteins, Membrane Proteins, Plant Proteins, Protein Kinases, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Aspartate Kinase, Histidine, Intracellular Signaling Peptides and Proteins, Membrane Proteins, Plant Proteins, Protein Kinases, Saccharomyces cerevisiae Proteins.
- genetics : Populus, Saccharomyces cerevisiae.
- growth & development : Saccharomyces cerevisiae.
- metabolism : Populus, Saccharomyces cerevisiae.
- Amino Acid Sequence, Blotting, Western, Genetic Complementation Test, Histidine Kinase, Molecular Sequence Data, Mutation, Phosphorylation, Protein Binding, Protein Multimerization, Sequence Homology, Amino Acid, Two-Hybrid System Techniques.
Abstract
In poplar, we identified proteins homologous to yeast proteins involved in osmosensing multistep phosphorelay Sln1p-Ypd1p-Ssk1p. This finding led us to speculate that Populus cells could sense osmotic stress by a similar mechanism. This study focuses on first and second protagonists of this possible pathway: a histidine-aspartate kinase (HK1), putative osmosensor and histidine phosphotransfer proteins (HPt1 to 10), potential partners of this HK. Characterization of HK1 showed its ability to homodimerize in two-hybrid tests and to act as an osmosensor with a kinase activity in yeast, by functional complementation of sln1Δ sho1Δ strain. Moreover, in plant cells, plasma membrane localization of HK1 is shown. Further analysis on HPts allowed us to isolate seven new cDNAs, leading to a total of 10 different HPts identified in poplar. Interaction tests showed that almost all HPts can interact with HK1, but two of them exhibit stronger interactions, suggesting a preferential partnership in poplar. The importance of the phosphorylation status in these interactions has been investigated with two-hybrid tests carried out with mutated HK1 forms. Finally, in planta co-expression analysis of genes encoding these potential partners revealed that only three HPts are co-expressed with HK1 in different poplar organs. This result reinforces the hypothesis of a partnership between HK1 and these three preferential HPts in planta. Taken together, these results shed some light on proteins partnerships that could be involved in the osmosensing pathway in Populus.
DOI: 10.1111/ppl.12024
PubMed: 23330606
Links to Exploration step
pubmed:23330606Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Characterization of histidine-aspartate kinase HK1 and identification of histidine phosphotransfer proteins as potential partners in a Populus multistep phosphorelay.</title><author><name sortKey="Hericourt, Francois" sort="Hericourt, Francois" uniqKey="Hericourt F" first="François" last="Héricourt">François Héricourt</name><affiliation><nlm:affiliation>Université d'Orléans, UPRES EA 1207, Laboratoire de Biologie des Ligneux et des Grandes Cultures (LBLGC), 45067, Orléans Cedex 2, France; INRA, USC1328, Arbres et Réponses aux Contraintes Hydriques et Environnementales (ARCHE), 45067, Orléans Cedex 2, France.</nlm:affiliation></affiliation></author><author><name sortKey="Chefdor, Francoise" sort="Chefdor, Francoise" uniqKey="Chefdor F" first="Françoise" last="Chefdor">Françoise Chefdor</name></author><author><name sortKey="Bertheau, Lucie" sort="Bertheau, Lucie" uniqKey="Bertheau L" first="Lucie" last="Bertheau">Lucie Bertheau</name></author><author><name sortKey="Tanigawa, Mirai" sort="Tanigawa, Mirai" uniqKey="Tanigawa M" first="Mirai" last="Tanigawa">Mirai Tanigawa</name></author><author><name sortKey="Maeda, Tatsuya" sort="Maeda, Tatsuya" uniqKey="Maeda T" first="Tatsuya" last="Maeda">Tatsuya Maeda</name></author><author><name sortKey="Guirimand, Gregory" sort="Guirimand, Gregory" uniqKey="Guirimand G" first="Grégory" last="Guirimand">Grégory Guirimand</name></author><author><name sortKey="Courdavault, Vincent" sort="Courdavault, Vincent" uniqKey="Courdavault V" first="Vincent" last="Courdavault">Vincent Courdavault</name></author><author><name sortKey="Larcher, Melanie" sort="Larcher, Melanie" uniqKey="Larcher M" first="Mélanie" last="Larcher">Mélanie Larcher</name></author><author><name sortKey="Depierreux, Christiane" sort="Depierreux, Christiane" uniqKey="Depierreux C" first="Christiane" last="Depierreux">Christiane Depierreux</name></author><author><name sortKey="Benedetti, Helene" sort="Benedetti, Helene" uniqKey="Benedetti H" first="Hélène" last="Bénédetti">Hélène Bénédetti</name></author><author><name sortKey="Morabito, Domenico" sort="Morabito, Domenico" uniqKey="Morabito D" first="Domenico" last="Morabito">Domenico Morabito</name></author><author><name sortKey="Brignolas, Franck" sort="Brignolas, Franck" uniqKey="Brignolas F" first="Franck" last="Brignolas">Franck Brignolas</name></author><author><name sortKey="Carpin, Sabine" sort="Carpin, Sabine" uniqKey="Carpin S" first="Sabine" last="Carpin">Sabine Carpin</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2013">2013</date><idno type="RBID">pubmed:23330606</idno><idno type="pmid">23330606</idno><idno type="doi">10.1111/ppl.12024</idno><idno type="wicri:Area/Main/Corpus">002727</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">002727</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Characterization of histidine-aspartate kinase HK1 and identification of histidine phosphotransfer proteins as potential partners in a Populus multistep phosphorelay.</title><author><name sortKey="Hericourt, Francois" sort="Hericourt, Francois" uniqKey="Hericourt F" first="François" last="Héricourt">François Héricourt</name><affiliation><nlm:affiliation>Université d'Orléans, UPRES EA 1207, Laboratoire de Biologie des Ligneux et des Grandes Cultures (LBLGC), 45067, Orléans Cedex 2, France; INRA, USC1328, Arbres et Réponses aux Contraintes Hydriques et Environnementales (ARCHE), 45067, Orléans Cedex 2, France.</nlm:affiliation></affiliation></author><author><name sortKey="Chefdor, Francoise" sort="Chefdor, Francoise" uniqKey="Chefdor F" first="Françoise" last="Chefdor">Françoise Chefdor</name></author><author><name sortKey="Bertheau, Lucie" sort="Bertheau, Lucie" uniqKey="Bertheau L" first="Lucie" last="Bertheau">Lucie Bertheau</name></author><author><name sortKey="Tanigawa, Mirai" sort="Tanigawa, Mirai" uniqKey="Tanigawa M" first="Mirai" last="Tanigawa">Mirai Tanigawa</name></author><author><name sortKey="Maeda, Tatsuya" sort="Maeda, Tatsuya" uniqKey="Maeda T" first="Tatsuya" last="Maeda">Tatsuya Maeda</name></author><author><name sortKey="Guirimand, Gregory" sort="Guirimand, Gregory" uniqKey="Guirimand G" first="Grégory" last="Guirimand">Grégory Guirimand</name></author><author><name sortKey="Courdavault, Vincent" sort="Courdavault, Vincent" uniqKey="Courdavault V" first="Vincent" last="Courdavault">Vincent Courdavault</name></author><author><name sortKey="Larcher, Melanie" sort="Larcher, Melanie" uniqKey="Larcher M" first="Mélanie" last="Larcher">Mélanie Larcher</name></author><author><name sortKey="Depierreux, Christiane" sort="Depierreux, Christiane" uniqKey="Depierreux C" first="Christiane" last="Depierreux">Christiane Depierreux</name></author><author><name sortKey="Benedetti, Helene" sort="Benedetti, Helene" uniqKey="Benedetti H" first="Hélène" last="Bénédetti">Hélène Bénédetti</name></author><author><name sortKey="Morabito, Domenico" sort="Morabito, Domenico" uniqKey="Morabito D" first="Domenico" last="Morabito">Domenico Morabito</name></author><author><name sortKey="Brignolas, Franck" sort="Brignolas, Franck" uniqKey="Brignolas F" first="Franck" last="Brignolas">Franck Brignolas</name></author><author><name sortKey="Carpin, Sabine" sort="Carpin, Sabine" uniqKey="Carpin S" first="Sabine" last="Carpin">Sabine Carpin</name></author></analytic><series><title level="j">Physiologia plantarum</title><idno type="eISSN">1399-3054</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Aspartate Kinase (chemistry)</term><term>Aspartate Kinase (genetics)</term><term>Aspartate Kinase (metabolism)</term><term>Blotting, Western (MeSH)</term><term>Genetic Complementation Test (MeSH)</term><term>Histidine (genetics)</term><term>Histidine (metabolism)</term><term>Histidine Kinase (MeSH)</term><term>Intracellular Signaling Peptides and Proteins (genetics)</term><term>Intracellular Signaling Peptides and Proteins (metabolism)</term><term>Membrane Proteins (genetics)</term><term>Membrane Proteins (metabolism)</term><term>Molecular Sequence Data (MeSH)</term><term>Mutation (MeSH)</term><term>Phosphorylation (MeSH)</term><term>Plant Proteins (chemistry)</term><term>Plant Proteins (genetics)</term><term>Plant Proteins (metabolism)</term><term>Populus (genetics)</term><term>Populus (metabolism)</term><term>Protein Binding (MeSH)</term><term>Protein Kinases (chemistry)</term><term>Protein Kinases (genetics)</term><term>Protein Kinases (metabolism)</term><term>Protein Multimerization (MeSH)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Saccharomyces cerevisiae (growth & development)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (genetics)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Two-Hybrid System Techniques (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Aspartate Kinase</term><term>Plant Proteins</term><term>Protein Kinases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Aspartate Kinase</term><term>Histidine</term><term>Intracellular Signaling Peptides and Proteins</term><term>Membrane Proteins</term><term>Plant Proteins</term><term>Protein Kinases</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Aspartate Kinase</term><term>Histidine</term><term>Intracellular Signaling Peptides and Proteins</term><term>Membrane Proteins</term><term>Plant Proteins</term><term>Protein Kinases</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Populus</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Populus</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Blotting, Western</term><term>Genetic Complementation Test</term><term>Histidine Kinase</term><term>Molecular Sequence Data</term><term>Mutation</term><term>Phosphorylation</term><term>Protein Binding</term><term>Protein Multimerization</term><term>Sequence Homology, Amino Acid</term><term>Two-Hybrid System Techniques</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In poplar, we identified proteins homologous to yeast proteins involved in osmosensing multistep phosphorelay Sln1p-Ypd1p-Ssk1p. This finding led us to speculate that Populus cells could sense osmotic stress by a similar mechanism. This study focuses on first and second protagonists of this possible pathway: a histidine-aspartate kinase (HK1), putative osmosensor and histidine phosphotransfer proteins (HPt1 to 10), potential partners of this HK. Characterization of HK1 showed its ability to homodimerize in two-hybrid tests and to act as an osmosensor with a kinase activity in yeast, by functional complementation of sln1Δ sho1Δ strain. Moreover, in plant cells, plasma membrane localization of HK1 is shown. Further analysis on HPts allowed us to isolate seven new cDNAs, leading to a total of 10 different HPts identified in poplar. Interaction tests showed that almost all HPts can interact with HK1, but two of them exhibit stronger interactions, suggesting a preferential partnership in poplar. The importance of the phosphorylation status in these interactions has been investigated with two-hybrid tests carried out with mutated HK1 forms. Finally, in planta co-expression analysis of genes encoding these potential partners revealed that only three HPts are co-expressed with HK1 in different poplar organs. This result reinforces the hypothesis of a partnership between HK1 and these three preferential HPts in planta. Taken together, these results shed some light on proteins partnerships that could be involved in the osmosensing pathway in Populus. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23330606</PMID><DateCompleted><Year>2014</Year><Month>04</Month><Day>21</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1399-3054</ISSN><JournalIssue CitedMedium="Internet"><Volume>149</Volume><Issue>2</Issue><PubDate><Year>2013</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Physiologia plantarum</Title><ISOAbbreviation>Physiol Plant</ISOAbbreviation></Journal><ArticleTitle>Characterization of histidine-aspartate kinase HK1 and identification of histidine phosphotransfer proteins as potential partners in a Populus multistep phosphorelay.</ArticleTitle><Pagination><MedlinePgn>188-99</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1111/ppl.12024</ELocationID><Abstract><AbstractText>In poplar, we identified proteins homologous to yeast proteins involved in osmosensing multistep phosphorelay Sln1p-Ypd1p-Ssk1p. This finding led us to speculate that Populus cells could sense osmotic stress by a similar mechanism. This study focuses on first and second protagonists of this possible pathway: a histidine-aspartate kinase (HK1), putative osmosensor and histidine phosphotransfer proteins (HPt1 to 10), potential partners of this HK. Characterization of HK1 showed its ability to homodimerize in two-hybrid tests and to act as an osmosensor with a kinase activity in yeast, by functional complementation of sln1Δ sho1Δ strain. Moreover, in plant cells, plasma membrane localization of HK1 is shown. Further analysis on HPts allowed us to isolate seven new cDNAs, leading to a total of 10 different HPts identified in poplar. Interaction tests showed that almost all HPts can interact with HK1, but two of them exhibit stronger interactions, suggesting a preferential partnership in poplar. The importance of the phosphorylation status in these interactions has been investigated with two-hybrid tests carried out with mutated HK1 forms. Finally, in planta co-expression analysis of genes encoding these potential partners revealed that only three HPts are co-expressed with HK1 in different poplar organs. This result reinforces the hypothesis of a partnership between HK1 and these three preferential HPts in planta. Taken together, these results shed some light on proteins partnerships that could be involved in the osmosensing pathway in Populus. </AbstractText><CopyrightInformation>© 2013 Scandinavian Plant Physiology Society.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Héricourt</LastName><ForeName>François</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Université d'Orléans, UPRES EA 1207, Laboratoire de Biologie des Ligneux et des Grandes Cultures (LBLGC), 45067, Orléans Cedex 2, France; INRA, USC1328, Arbres et Réponses aux Contraintes Hydriques et Environnementales (ARCHE), 45067, Orléans Cedex 2, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chefdor</LastName><ForeName>Françoise</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Bertheau</LastName><ForeName>Lucie</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Tanigawa</LastName><ForeName>Mirai</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Maeda</LastName><ForeName>Tatsuya</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Guirimand</LastName><ForeName>Grégory</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Courdavault</LastName><ForeName>Vincent</ForeName><Initials>V</Initials></Author><Author ValidYN="Y"><LastName>Larcher</LastName><ForeName>Mélanie</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Depierreux</LastName><ForeName>Christiane</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Bénédetti</LastName><ForeName>Hélène</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Morabito</LastName><ForeName>Domenico</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Brignolas</LastName><ForeName>Franck</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Carpin</LastName><ForeName>Sabine</ForeName><Initials>S</Initials></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>2013</Year><Month>02</Month><Day>23</Day></ArticleDate></Article><MedlineJournalInfo><Country>Denmark</Country><MedlineTA>Physiol Plant</MedlineTA><NlmUniqueID>1256322</NlmUniqueID><ISSNLinking>0031-9317</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D047908">Intracellular Signaling Peptides and Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008565">Membrane Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C459787">SHO1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>4QD397987E</RegistryNumber><NameOfSubstance UI="D006639">Histidine</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.-</RegistryNumber><NameOfSubstance UI="D011494">Protein Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.-</RegistryNumber><NameOfSubstance UI="C102035">YPD1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.13.1</RegistryNumber><NameOfSubstance UI="D000071677">Histidine Kinase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.13.3</RegistryNumber><NameOfSubstance UI="C083749">SLN1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.2.4</RegistryNumber><NameOfSubstance UI="D001222">Aspartate Kinase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001222" MajorTopicYN="N">Aspartate Kinase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015153" MajorTopicYN="N">Blotting, Western</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005816" MajorTopicYN="N">Genetic Complementation Test</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006639" MajorTopicYN="N">Histidine</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000071677" MajorTopicYN="N">Histidine Kinase</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D047908" MajorTopicYN="N">Intracellular Signaling Peptides and Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008565" MajorTopicYN="N">Membrane Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010766" MajorTopicYN="N">Phosphorylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011494" MajorTopicYN="N">Protein Kinases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D055503" MajorTopicYN="N">Protein Multimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020798" MajorTopicYN="N">Two-Hybrid System Techniques</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2012</Year><Month>10</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2012</Year><Month>12</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2012</Year><Month>12</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>1</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>1</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>4</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23330606</ArticleId><ArticleId IdType="doi">10.1111/ppl.12024</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/PoplarV1/Data/Main/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002727 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Corpus/biblio.hfd -nk 002727 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= PoplarV1
|flux= Main
|étape= Corpus
|type= RBID
|clé= pubmed:23330606
|texte= Characterization of histidine-aspartate kinase HK1 and identification of histidine phosphotransfer proteins as potential partners in a Populus multistep phosphorelay.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Corpus/RBID.i -Sk "pubmed:23330606" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Corpus/biblio.hfd \
| NlmPubMed2Wicri -a PoplarV1
| This area was generated with Dilib version V0.6.37. |  |