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Titolo:
Rapid evolution in plant chitinases: Molecular targets of selection in plant-pathogen coevolution
Autore:
Bishop, JG; Dean, AM; Mitchell-Olds, T;
Indirizzi:
Washington State Univ, Sch Biol Sci, Vancouver, WA 98686 USA Washington State Univ Vancouver WA USA 98686 Sci, Vancouver, WA 98686 USA Max Planck Inst Chem Ecol, D-07745 Jena, Germany Max Planck Inst Chem Ecol Jena Germany D-07745 ol, D-07745 Jena, Germany Univ Minnesota, Dept Ecol Evolut & Behav, St Paul, MN 55108 USA Univ Minnesota St Paul MN USA 55108 Evolut & Behav, St Paul, MN 55108 USA Univ Minnesota, Biol Proc Technol Inst, St Paul, MN 55108 USA Univ Minnesota St Paul MN USA 55108 c Technol Inst, St Paul, MN 55108 USA
Titolo Testata:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
fascicolo: 10, volume: 97, anno: 2000,
pagine: 5322 - 5327
SICI:
0027-8424(20000509)97:10<5322:REIPCM>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
DOWNY MILDEW RESISTANCE; ARABIDOPSIS-THALIANA; POSITIVE SELECTION; ADAPTIVE EVOLUTION; TOBACCO; GENES; LYSOZYME; BINDING; SUBSTITUTION; ALLOSAMIDIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
53
Recensione:
Indirizzi per estratti:
Indirizzo: Bishop, JG Washington State Univ, Sch Biol Sci, 14204 NE Salmon Creek Ave,Vancouver,WA 98686 USA Washington State Univ 14204 NE Salmon Creek Ave Vancouver WA USA 98686
Citazione:
J.G. Bishop et al., "Rapid evolution in plant chitinases: Molecular targets of selection in plant-pathogen coevolution", P NAS US, 97(10), 2000, pp. 5322-5327

Abstract

Many pathogen recognition genes, such as plant R-genes, undergo rapid adaptive evolution, providing evidence that these genes play a critical role inplant-pathogen coevolution. Surprisingly, whether rapid adaptive evolutionalso occurs in genes encoding other kinds of plant defense proteins is unknown. Unlike recognition proteins, plant chitinases attack pathogens directly, conferring disease resistance by degrading chitin, a component of fungal cell walls. Here, we show that nonsynonymous substitution rates in plant class I chitinase often exceed synonymous rates in the plant genus Arabis (Cruciferae) and in other dicots, indicating a succession of adaptively driven amino acid replacements. We identify individual residues that are likelysubject to positive selection by using codon substitution models and determine the location of these residues on the three-dimensional structure of class I chitinase. In contrast to primate lysozymes and plant class III chitinases, structural and functional relatives of class I chitinase, the adaptive replacements of class I chitinase occur disproportionately in the active site deft This highly unusual pattern of replacements suggests that fungidirectly defend against chitinolytic activity through enzymatic inhibitionor other forms of chemical resistance and identifies target residues for manipulating chitinolytic activity. These data also provide empirical evidence that plant defense proteins not involved in pathogen recognition also evolve in a manner consistent with rapid coevolutionary interactions.

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Documento generato il 26/09/20 alle ore 14:20:43