A novel nuclear protein interacts with the symbiotic DMI3 calcium- and calmodulin-dependent protein kinase of Medicago truncatula.
Identifieur interne : 002E53 ( Main/Corpus ); précédent : 002E52; suivant : 002E54A novel nuclear protein interacts with the symbiotic DMI3 calcium- and calmodulin-dependent protein kinase of Medicago truncatula.
Auteurs : Elsa Messinese ; Jeong-Hwan Mun ; Li Huey Yeun ; Dhileepkumar Jayaraman ; Pierre Rougé ; Annick Barre ; Géraldine Lougnon ; Sebastian Schornack ; Jean-Jacques Bono ; Douglas R. Cook ; Jean-Michel AnéSource :
- Molecular plant-microbe interactions : MPMI [ 0894-0282 ] ; 2007.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Calcium-Calmodulin-Dependent Protein Kinases (genetics), Calcium-Calmodulin-Dependent Protein Kinases (metabolism), Conserved Sequence (MeSH), Green Fluorescent Proteins (analysis), Medicago truncatula (enzymology), Medicago truncatula (microbiology), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Mycorrhizae (physiology), Plant Proteins (chemistry), Plant Proteins (metabolism), Plant Proteins (physiology), RNA Interference (MeSH), Root Nodules, Plant (genetics), Root Nodules, Plant (metabolism), Root Nodules, Plant (microbiology), Sequence Alignment (MeSH), Symbiosis (physiology), Two-Hybrid System Techniques (MeSH).
- MESH :
- chemical , analysis : Green Fluorescent Proteins.
- chemical , chemistry : Plant Proteins.
- chemical , genetics : Calcium-Calmodulin-Dependent Protein Kinases.
- chemical , metabolism : Calcium-Calmodulin-Dependent Protein Kinases, Plant Proteins.
- enzymology : Medicago truncatula.
- genetics : Root Nodules, Plant.
- metabolism : Root Nodules, Plant.
- microbiology : Medicago truncatula, Root Nodules, Plant.
- physiology : Mycorrhizae, Plant Proteins, Symbiosis.
- Amino Acid Sequence, Conserved Sequence, Models, Molecular, Molecular Sequence Data, RNA Interference, Sequence Alignment, Two-Hybrid System Techniques.
Abstract
Many higher plants establish symbiotic relationships with arbuscular mycorrhizal (AM) fungi that improve their ability to acquire nutrients from the soil. In addition to establishing AM symbiosis, legumes also enter into a nitrogen-fixing symbiosis with bacteria known as rhizobia that results in the formation of root nodules. Several genes involved in the perception and transduction of bacterial symbiotic signals named "Nod factors" have been cloned recently in model legumes through forward genetic approaches. Among them, DMI3 (Doesn't Make Infections 3) is a calcium- and calmodulin-dependent kinase required for the establishment of both nodulation and AM symbiosis. We have identified, by a yeast two-hybrid system, a novel protein interacting with DMI3 named IPD3 (Interacting Protein of DMI3). IPD3 is predicted to interact with DMI3 through a C-terminal coiled-coil domain. Chimeric IPD3::GFP is localized to the nucleus of transformed Medicago truncatula root cells, in which split yellow fluorescent protein assays suggest that IPD3 and DMI3 physically interact in Nicotiana benthamiana. Like DMI3, IPD3 is extremely well conserved among the angiosperms and is absent from Arabidopsis. Despite this high level of conservation, none of the homologous proteins have a demonstrated biological or biochemical function. This work provides the first evidence of the involvement of IPD3 in a nuclear interaction with DMI3.
DOI: 10.1094/MPMI-20-8-0912
PubMed: 17722695
Links to Exploration step
pubmed:17722695Le document en format XML
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Cook</name></author><author><name sortKey="Ane, Jean Michel" sort="Ane, Jean Michel" uniqKey="Ane J" first="Jean-Michel" last="Ané">Jean-Michel Ané</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2007">2007</date><idno type="RBID">pubmed:17722695</idno><idno type="pmid">17722695</idno><idno type="doi">10.1094/MPMI-20-8-0912</idno><idno type="wicri:Area/Main/Corpus">002E53</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">002E53</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">A novel nuclear protein interacts with the symbiotic DMI3 calcium- and calmodulin-dependent protein kinase of Medicago truncatula.</title><author><name sortKey="Messinese, Elsa" sort="Messinese, Elsa" uniqKey="Messinese E" first="Elsa" last="Messinese">Elsa Messinese</name><affiliation><nlm:affiliation>Department of Agronomy, University of Wisconsin, 1575 Linden Drive, Madison, WI 53706, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Mun, Jeong Hwan" sort="Mun, Jeong Hwan" uniqKey="Mun J" first="Jeong-Hwan" last="Mun">Jeong-Hwan Mun</name></author><author><name sortKey="Yeun, Li Huey" sort="Yeun, Li Huey" uniqKey="Yeun L" first="Li Huey" last="Yeun">Li Huey Yeun</name></author><author><name sortKey="Jayaraman, Dhileepkumar" sort="Jayaraman, Dhileepkumar" uniqKey="Jayaraman D" first="Dhileepkumar" last="Jayaraman">Dhileepkumar Jayaraman</name></author><author><name sortKey="Rouge, Pierre" sort="Rouge, Pierre" uniqKey="Rouge P" first="Pierre" last="Rougé">Pierre Rougé</name></author><author><name sortKey="Barre, Annick" sort="Barre, Annick" uniqKey="Barre A" first="Annick" last="Barre">Annick Barre</name></author><author><name sortKey="Lougnon, Geraldine" sort="Lougnon, Geraldine" uniqKey="Lougnon G" first="Géraldine" last="Lougnon">Géraldine Lougnon</name></author><author><name sortKey="Schornack, Sebastian" sort="Schornack, Sebastian" uniqKey="Schornack S" first="Sebastian" last="Schornack">Sebastian Schornack</name></author><author><name sortKey="Bono, Jean Jacques" sort="Bono, Jean Jacques" uniqKey="Bono J" first="Jean-Jacques" last="Bono">Jean-Jacques Bono</name></author><author><name sortKey="Cook, Douglas R" sort="Cook, Douglas R" uniqKey="Cook D" first="Douglas R" last="Cook">Douglas R. Cook</name></author><author><name sortKey="Ane, Jean Michel" sort="Ane, Jean Michel" uniqKey="Ane J" first="Jean-Michel" last="Ané">Jean-Michel Ané</name></author></analytic><series><title level="j">Molecular plant-microbe interactions : MPMI</title><idno type="ISSN">0894-0282</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Calcium-Calmodulin-Dependent Protein Kinases (genetics)</term><term>Calcium-Calmodulin-Dependent Protein Kinases (metabolism)</term><term>Conserved Sequence (MeSH)</term><term>Green Fluorescent Proteins (analysis)</term><term>Medicago truncatula (enzymology)</term><term>Medicago truncatula (microbiology)</term><term>Models, Molecular (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Mycorrhizae (physiology)</term><term>Plant Proteins (chemistry)</term><term>Plant Proteins (metabolism)</term><term>Plant Proteins (physiology)</term><term>RNA Interference (MeSH)</term><term>Root Nodules, Plant (genetics)</term><term>Root Nodules, Plant (metabolism)</term><term>Root Nodules, Plant (microbiology)</term><term>Sequence Alignment (MeSH)</term><term>Symbiosis (physiology)</term><term>Two-Hybrid System Techniques (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Green Fluorescent Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Plant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Calcium-Calmodulin-Dependent Protein Kinases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Calcium-Calmodulin-Dependent Protein Kinases</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Medicago truncatula</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Root Nodules, Plant</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Root Nodules, Plant</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Medicago truncatula</term><term>Root Nodules, Plant</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Mycorrhizae</term><term>Plant Proteins</term><term>Symbiosis</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Conserved Sequence</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>RNA Interference</term><term>Sequence Alignment</term><term>Two-Hybrid System Techniques</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Many higher plants establish symbiotic relationships with arbuscular mycorrhizal (AM) fungi that improve their ability to acquire nutrients from the soil. In addition to establishing AM symbiosis, legumes also enter into a nitrogen-fixing symbiosis with bacteria known as rhizobia that results in the formation of root nodules. Several genes involved in the perception and transduction of bacterial symbiotic signals named "Nod factors" have been cloned recently in model legumes through forward genetic approaches. Among them, DMI3 (Doesn't Make Infections 3) is a calcium- and calmodulin-dependent kinase required for the establishment of both nodulation and AM symbiosis. We have identified, by a yeast two-hybrid system, a novel protein interacting with DMI3 named IPD3 (Interacting Protein of DMI3). IPD3 is predicted to interact with DMI3 through a C-terminal coiled-coil domain. Chimeric IPD3::GFP is localized to the nucleus of transformed Medicago truncatula root cells, in which split yellow fluorescent protein assays suggest that IPD3 and DMI3 physically interact in Nicotiana benthamiana. Like DMI3, IPD3 is extremely well conserved among the angiosperms and is absent from Arabidopsis. Despite this high level of conservation, none of the homologous proteins have a demonstrated biological or biochemical function. This work provides the first evidence of the involvement of IPD3 in a nuclear interaction with DMI3.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17722695</PMID><DateCompleted><Year>2007</Year><Month>12</Month><Day>20</Day></DateCompleted><DateRevised><Year>2007</Year><Month>08</Month><Day>28</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0894-0282</ISSN><JournalIssue CitedMedium="Print"><Volume>20</Volume><Issue>8</Issue><PubDate><Year>2007</Year><Month>Aug</Month></PubDate></JournalIssue><Title>Molecular plant-microbe interactions : MPMI</Title><ISOAbbreviation>Mol Plant Microbe Interact</ISOAbbreviation></Journal><ArticleTitle>A novel nuclear protein interacts with the symbiotic DMI3 calcium- and calmodulin-dependent protein kinase of Medicago truncatula.</ArticleTitle><Pagination><MedlinePgn>912-21</MedlinePgn></Pagination><Abstract><AbstractText>Many higher plants establish symbiotic relationships with arbuscular mycorrhizal (AM) fungi that improve their ability to acquire nutrients from the soil. In addition to establishing AM symbiosis, legumes also enter into a nitrogen-fixing symbiosis with bacteria known as rhizobia that results in the formation of root nodules. Several genes involved in the perception and transduction of bacterial symbiotic signals named "Nod factors" have been cloned recently in model legumes through forward genetic approaches. Among them, DMI3 (Doesn't Make Infections 3) is a calcium- and calmodulin-dependent kinase required for the establishment of both nodulation and AM symbiosis. We have identified, by a yeast two-hybrid system, a novel protein interacting with DMI3 named IPD3 (Interacting Protein of DMI3). IPD3 is predicted to interact with DMI3 through a C-terminal coiled-coil domain. Chimeric IPD3::GFP is localized to the nucleus of transformed Medicago truncatula root cells, in which split yellow fluorescent protein assays suggest that IPD3 and DMI3 physically interact in Nicotiana benthamiana. Like DMI3, IPD3 is extremely well conserved among the angiosperms and is absent from Arabidopsis. Despite this high level of conservation, none of the homologous proteins have a demonstrated biological or biochemical function. This work provides the first evidence of the involvement of IPD3 in a nuclear interaction with DMI3.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Messinese</LastName><ForeName>Elsa</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Department of Agronomy, University of Wisconsin, 1575 Linden Drive, Madison, WI 53706, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mun</LastName><ForeName>Jeong-Hwan</ForeName><Initials>JH</Initials></Author><Author ValidYN="Y"><LastName>Yeun</LastName><ForeName>Li Huey</ForeName><Initials>LH</Initials></Author><Author ValidYN="Y"><LastName>Jayaraman</LastName><ForeName>Dhileepkumar</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Rougé</LastName><ForeName>Pierre</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Barre</LastName><ForeName>Annick</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Lougnon</LastName><ForeName>Géraldine</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Schornack</LastName><ForeName>Sebastian</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Bono</LastName><ForeName>Jean-Jacques</ForeName><Initials>JJ</Initials></Author><Author ValidYN="Y"><LastName>Cook</LastName><ForeName>Douglas R</ForeName><Initials>DR</Initials></Author><Author ValidYN="Y"><LastName>Ané</LastName><ForeName>Jean-Michel</ForeName><Initials>JM</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>GENBANK</DataBankName><AccessionNumberList><AccessionNumber>EF117279</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Mol Plant Microbe Interact</MedlineTA><NlmUniqueID>9107902</NlmUniqueID><ISSNLinking>0894-0282</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>147336-22-9</RegistryNumber><NameOfSubstance UI="D049452">Green Fluorescent Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.17</RegistryNumber><NameOfSubstance UI="D017871">Calcium-Calmodulin-Dependent Protein Kinases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017871" MajorTopicYN="N">Calcium-Calmodulin-Dependent Protein Kinases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017124" MajorTopicYN="N">Conserved Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D049452" MajorTopicYN="N">Green Fluorescent Proteins</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D046913" MajorTopicYN="N">Medicago truncatula</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D038821" MajorTopicYN="N">Mycorrhizae</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D034622" MajorTopicYN="N">RNA Interference</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D053204" MajorTopicYN="N">Root Nodules, Plant</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013559" MajorTopicYN="N">Symbiosis</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020798" MajorTopicYN="N">Two-Hybrid System Techniques</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>8</Month><Day>29</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>12</Month><Day>21</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>8</Month><Day>29</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17722695</ArticleId><ArticleId IdType="doi">10.1094/MPMI-20-8-0912</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour 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