Structurefunction analysis of the NB-ARC domain of plant disease resistance proteins
Identifieur interne : 000628 ( Main/Exploration ); précédent : 000627; suivant : 000629Structurefunction analysis of the NB-ARC domain of plant disease resistance proteins
Auteurs : Gerben Van Ooijen [Pays-Bas] ; Gabriele Mayr [Allemagne] ; Mobien M. A. Kasiem [Pays-Bas] ; Mario Albrecht [Allemagne] ; Ben J. C. Cornelissen [Pays-Bas] ; Frank L. W. Takken [Pays-Bas]Source :
- Journal of Experimental Botany [ 0022-0957 ] ; 2008-04-04.
Abstract
Resistance (R) proteins in plants are involved in pathogen recognition and subsequent activation of innate immune responses. Most resistance proteins contain a central nucleotide-binding domain. This so-called NB-ARC domain consists of three subdomains: NB, ARC1, and ARC2. The NB-ARC domain is a functional ATPase domain, and its nucleotide-binding state is proposed to regulate activity of the R protein. A highly conserved methioninehistidineaspartate (MHD) motif is present at the carboxy-terminus of ARC2. An extensive mutational analysis of the MHD motif in the R proteins I-2 and Mi-1 is reported. Several novel autoactivating mutations of the MHD invariant histidine and conserved aspartate were identified. The combination of MHD mutants with autoactivating hydrolysis mutants in the NB subdomain showed that the autoactivation phenotypes are not additive. This finding indicates an important regulatory role for the MHD motif in the control of R protein activity. To explain these observations, a three-dimensional model of the NB-ARC domain of I-2 was built, based on the APAF-1 template structure. The model was used to identify residues important for I-2 function. Substitution of the selected residues resulted in the expected distinct phenotypes. Based on the model, it is proposed that the MHD motif fulfils the same function as the sensor II motif found in AAA proteins (ATPases associated with diverse cellular activities)co-ordination of the nucleotide and control of subdomain interactions. The presented 3D model provides a framework for the formulation of hypotheses on how mutations in the NB-ARC exert their effects.
Url:
DOI: 10.1093/jxb/ern045
Affiliations:
- Allemagne, Pays-Bas
- Hollande-Septentrionale, Sarre (Land)
- Amsterdam, Sarrebruck
- Université d'Amsterdam
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Takken</name><affiliation wicri:level="4"><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Plant Pathology, Swammerdam Institute for Life Sciences, University of Amsterdam, PO Box 94062, 1090 GB Amsterdam</wicri:regionArea><orgName type="university">Université d'Amsterdam</orgName><placeName><settlement type="city">Amsterdam</settlement><region>Hollande-Septentrionale</region></placeName></affiliation><affiliation wicri:level="1"><country wicri:rule="url">Pays-Bas</country></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Experimental Botany</title><idno type="ISSN">0022-0957</idno><idno type="eISSN">1460-2431</idno><imprint><publisher>Oxford University Press</publisher><date type="published" when="2008-04-04">2008-04-04</date><biblScope unit="volume">59</biblScope><biblScope unit="issue">6</biblScope><biblScope unit="page" from="1383">1383</biblScope><biblScope unit="page" to="1397">1397</biblScope></imprint><idno type="ISSN">0022-0957</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0022-0957</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract">Resistance (R) proteins in plants are involved in pathogen recognition and subsequent activation of innate immune responses. Most resistance proteins contain a central nucleotide-binding domain. This so-called NB-ARC domain consists of three subdomains: NB, ARC1, and ARC2. The NB-ARC domain is a functional ATPase domain, and its nucleotide-binding state is proposed to regulate activity of the R protein. A highly conserved methioninehistidineaspartate (MHD) motif is present at the carboxy-terminus of ARC2. An extensive mutational analysis of the MHD motif in the R proteins I-2 and Mi-1 is reported. Several novel autoactivating mutations of the MHD invariant histidine and conserved aspartate were identified. The combination of MHD mutants with autoactivating hydrolysis mutants in the NB subdomain showed that the autoactivation phenotypes are not additive. This finding indicates an important regulatory role for the MHD motif in the control of R protein activity. To explain these observations, a three-dimensional model of the NB-ARC domain of I-2 was built, based on the APAF-1 template structure. The model was used to identify residues important for I-2 function. Substitution of the selected residues resulted in the expected distinct phenotypes. Based on the model, it is proposed that the MHD motif fulfils the same function as the sensor II motif found in AAA proteins (ATPases associated with diverse cellular activities)co-ordination of the nucleotide and control of subdomain interactions. The presented 3D model provides a framework for the formulation of hypotheses on how mutations in the NB-ARC exert their effects.</div></front></TEI><affiliations><list><country><li>Allemagne</li><li>Pays-Bas</li></country><region><li>Hollande-Septentrionale</li><li>Sarre (Land)</li></region><settlement><li>Amsterdam</li><li>Sarrebruck</li></settlement><orgName><li>Université d'Amsterdam</li></orgName></list><tree><country name="Pays-Bas"><region name="Hollande-Septentrionale"><name sortKey="Van Ooijen, Gerben" sort="Van Ooijen, Gerben" uniqKey="Van Ooijen G" first="Gerben" last="Van Ooijen">Gerben Van Ooijen</name></region><name sortKey="Cornelissen, Ben J C" sort="Cornelissen, Ben J C" uniqKey="Cornelissen B" first="Ben J. C." last="Cornelissen">Ben J. C. Cornelissen</name><name sortKey="Kasiem, Mobien M A" sort="Kasiem, Mobien M A" uniqKey="Kasiem M" first="Mobien M. A." last="Kasiem">Mobien M. A. Kasiem</name><name sortKey="Takken, Frank L W" sort="Takken, Frank L W" uniqKey="Takken F" first="Frank L. W." last="Takken">Frank L. W. Takken</name><name sortKey="Takken, Frank L W" sort="Takken, Frank L W" uniqKey="Takken F" first="Frank L. W." last="Takken">Frank L. W. Takken</name></country><country name="Allemagne"><region name="Sarre (Land)"><name sortKey="Mayr, Gabriele" sort="Mayr, Gabriele" uniqKey="Mayr G" first="Gabriele" last="Mayr">Gabriele Mayr</name></region><name sortKey="Albrecht, Mario" sort="Albrecht, Mario" uniqKey="Albrecht M" first="Mario" last="Albrecht">Mario Albrecht</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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