Arabidopsis thaliana Genes Encoding Defense Signaling and Recognition Proteins Exhibit Contrasting Evolutionary Dynamics
Autor: | Richard W Michelmore, Katherine S. Caldwell |
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Rok vydání: | 2009 |
Předmět: |
DNA
Plant Molecular Sequence Data Arabidopsis Protein Serine-Threonine Kinases Investigations Genes Plant Polymorphism Single Nucleotide DNA-binding protein Evolution Molecular Genetics Arabidopsis thaliana Selection Genetic Gene biology Arabidopsis Proteins Effector fungi Pattern recognition receptor food and beverages biology.organism_classification NPR1 DNA-Binding Proteins Host-Pathogen Interactions Signal transduction Carboxylic Ester Hydrolases Signal Transduction |
Zdroj: | Genetics. 181:671-684 |
ISSN: | 1943-2631 |
DOI: | 10.1534/genetics.108.097279 |
Popis: | The interplay between pathogen effectors, their host targets, and cognate recognition proteins provides various opportunities for antagonistic cycles of selection acting on plant and pathogen to achieve or abrogate resistance, respectively. Selection has previously been shown to maintain diversity in plant proteins involved in pathogen recognition and some of their cognate pathogen effectors. We analyzed the signatures of selection on 10 Arabidopsis thaliana genes encoding defense signal transduction proteins in plants, which are potential targets of pathogen effectors. There was insufficient evidence to reject neutral evolution for 6 genes encoding signaling components consistent with these proteins not being targets of effectors and/or indicative of constraints on their ability to coevolve with pathogen effectors. Functional constraints on effector targets may have provided the driving selective force for the evolution of guard proteins. PBS1, a known target of an effector, showed little variation but is known to be monitored by a variable guard protein. Evidence of selection maintaining diversity was present at NPR1, PAD4, and EDS1. Differences in the signatures of selection observed may reflect the numbers of effectors that target a particular protein, the presence or absence of a cognate guard protein, as well as functional constraints imposed by biochemical activities or interactions with plant proteins. |
Databáze: | OpenAIRE |
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