A novel nuclear protein interacts with the symbiotic DMI3 calcium- and calmodulin-dependent protein kinase of Medicago truncatula.
Identifieur interne : 002E53 ( Main/Curation ); précédent : 002E52; suivant : 002E54A novel nuclear protein interacts with the symbiotic DMI3 calcium- and calmodulin-dependent protein kinase of Medicago truncatula.
Auteurs : Elsa Messinese [États-Unis] ; 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.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Calcium-Calmodulin-Dependent Protein Kinases (génétique), Calcium-Calmodulin-Dependent Protein Kinases (métabolisme), Données de séquences moléculaires (MeSH), Interférence par ARN (MeSH), Medicago truncatula (enzymologie), Medicago truncatula (microbiologie), Modèles moléculaires (MeSH), Mycorhizes (physiologie), Nodules racinaires de plante (génétique), Nodules racinaires de plante (microbiologie), Nodules racinaires de plante (métabolisme), Protéines végétales (composition chimique), Protéines végétales (métabolisme), Protéines végétales (physiologie), Protéines à fluorescence verte (analyse), Symbiose (physiologie), Séquence conservée (MeSH), Séquence d'acides aminés (MeSH), Techniques de double hybride (MeSH).
- MESH :
- analyse : Protéines à fluorescence verte.
- composition chimique : Protéines végétales.
- enzymologie : Medicago truncatula.
- génétique : Calcium-Calmodulin-Dependent Protein Kinases, Nodules racinaires de plante.
- microbiologie : Medicago truncatula, Nodules racinaires de plante.
- métabolisme : Calcium-Calmodulin-Dependent Protein Kinases, Nodules racinaires de plante, Protéines végétales.
- physiologie : Mycorhizes, Protéines végétales, Symbiose.
- Alignement de séquences, Données de séquences moléculaires, Interférence par ARN, Modèles moléculaires, Séquence conservée, Séquence d'acides aminés, Techniques de double hybride.
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
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pubmed:17722695Le document en format XML
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<term>Conserved Sequence (MeSH)</term>
<term>Green Fluorescent Proteins (analysis)</term>
<term>Medicago truncatula (enzymology)</term>
<term>Medicago truncatula (microbiology)</term>
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<term>Molecular Sequence Data (MeSH)</term>
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<term>Plant Proteins (metabolism)</term>
<term>Plant Proteins (physiology)</term>
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<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>
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<term>Calcium-Calmodulin-Dependent Protein Kinases (métabolisme)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Interférence par ARN (MeSH)</term>
<term>Medicago truncatula (enzymologie)</term>
<term>Medicago truncatula (microbiologie)</term>
<term>Modèles moléculaires (MeSH)</term>
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<term>Nodules racinaires de plante (microbiologie)</term>
<term>Nodules racinaires de plante (métabolisme)</term>
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<term>Protéines végétales (métabolisme)</term>
<term>Protéines végétales (physiologie)</term>
<term>Protéines à fluorescence verte (analyse)</term>
<term>Symbiose (physiologie)</term>
<term>Séquence conservée (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
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<term>Nodules racinaires de plante</term>
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<term>Nodules racinaires de plante</term>
<term>Protéines végétales</term>
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<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Mycorhizes</term>
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<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>
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<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>
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