Identification of target amino acids that affect interactions of fungal polygalacturonases and their plant inhibitors
Identifieur interne : 002F42 ( Main/Exploration ); précédent : 002F41; suivant : 002F43Identification of target amino acids that affect interactions of fungal polygalacturonases and their plant inhibitors
Auteurs : Henrik U. Stotz [Allemagne] ; John G. Bishop [États-Unis] ; Carl W. Bergmann [États-Unis] ; Marcus Koch [Autriche] ; Peter Albersheim [États-Unis] ; Alan G. Darvill [États-Unis] ; John M. Labavitch [États-Unis]Source :
- Physiological and Molecular Plant Pathology [ 0885-5765 ] ; 2000.
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Abstract
Plant polygalacturonase inhibitor proteins (PGIPs) bind fungal polygalacturonases (PGs), but inhibition specificities and kinetics vary within and among species. Purified bean PGIP inhibited all fungal PGs we tested, includingFusarium moniliforme PG. Pear PGIP, however, was only effective against Botrytis cinerea PG. Moreover, tomato PGIP inhibited B. cinerea PG more than Aspergillus niger PG. Models of codon evolution for 22 dicot PGIPs and 19 fungal PGs indicated that advantageous substitutions dominate the molecular evolution of these genes and identified 9 amino acid residues, each, that are likely to evolve adaptively in response to natural selection. Many of these residues are within the β-strand/β-turn region of the PGIP LRR, including two sites known to alter inhibition specificities of bean PGIPs, but others lie outside this region. Our results complement existing molecular and biochemical studies of resistance specificity, and suggest new target amino acids for manipulating PG-inhibition.
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DOI: 10.1006/pmpp.2000.0258
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Labavitch</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pomology, University of California, Davis, CA, 95616</wicri:regionArea><wicri:noRegion>95616</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Physiological and Molecular Plant Pathology</title><title level="j" type="abbrev">YPMPP</title><idno type="ISSN">0885-5765</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="2000">2000</date><biblScope unit="volume">56</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="117">117</biblScope><biblScope unit="page" to="130">130</biblScope></imprint><idno type="ISSN">0885-5765</idno></series><idno type="istex">24E89CFD0AE88C4AC7096C4AB040D704FA463A49</idno><idno type="DOI">10.1006/pmpp.2000.0258</idno><idno type="PII">S0885-5765(00)90258-3</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0885-5765</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aspergillus niger</term><term>Botrytis cinerea</term><term>Fusarium moniliforme</term><term>Lycopersicon esculentum</term><term>Phaseolus vulgaris</term><term>Pyrus communis</term><term>evolution.</term><term>protein interaction</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Plant polygalacturonase inhibitor proteins (PGIPs) bind fungal polygalacturonases (PGs), but inhibition specificities and kinetics vary within and among species. Purified bean PGIP inhibited all fungal PGs we tested, includingFusarium moniliforme PG. Pear PGIP, however, was only effective against Botrytis cinerea PG. Moreover, tomato PGIP inhibited B. cinerea PG more than Aspergillus niger PG. Models of codon evolution for 22 dicot PGIPs and 19 fungal PGs indicated that advantageous substitutions dominate the molecular evolution of these genes and identified 9 amino acid residues, each, that are likely to evolve adaptively in response to natural selection. Many of these residues are within the β-strand/β-turn region of the PGIP LRR, including two sites known to alter inhibition specificities of bean PGIPs, but others lie outside this region. Our results complement existing molecular and biochemical studies of resistance specificity, and suggest new target amino acids for manipulating PG-inhibition.</div></front></TEI><affiliations><list><country><li>Allemagne</li><li>Autriche</li><li>États-Unis</li></country><region><li>Vienne (Autriche)</li></region><settlement><li>Vienne (Autriche)</li></settlement></list><tree><country name="Allemagne"><noRegion><name sortKey="Stotz, Henrik U" sort="Stotz, Henrik U" uniqKey="Stotz H" first="Henrik U" last="Stotz">Henrik U. Stotz</name></noRegion></country><country name="États-Unis"><noRegion><name sortKey="Bishop, John G" sort="Bishop, John G" uniqKey="Bishop J" first="John G" last="Bishop">John G. Bishop</name></noRegion><name sortKey="Albersheim, Peter" sort="Albersheim, Peter" uniqKey="Albersheim P" first="Peter" last="Albersheim">Peter Albersheim</name><name sortKey="Bergmann, Carl W" sort="Bergmann, Carl W" uniqKey="Bergmann C" first="Carl W" last="Bergmann">Carl W. Bergmann</name><name sortKey="Darvill, Alan G" sort="Darvill, Alan G" uniqKey="Darvill A" first="Alan G" last="Darvill">Alan G. Darvill</name><name sortKey="Labavitch, John M" sort="Labavitch, John M" uniqKey="Labavitch J" first="John M" last="Labavitch">John M. Labavitch</name></country><country name="Autriche"><region name="Vienne (Autriche)"><name sortKey="Koch, Marcus" sort="Koch, Marcus" uniqKey="Koch M" first="Marcus" last="Koch">Marcus Koch</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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