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Structural elucidation and functional characterization of the Hyaloperonospora arabidopsidis effector protein ATR13

Leonelli, Lauriebeth ; Pelton, Jeffery ; Schoeffler, Allyn ; Dahlbeck, Douglas ; Berger, James ; Wemmer, David E ; Staskawicz, Brian Tyler, Brett

PLoS pathogens, 2011-12, Vol.7 (12), p.e1002428 [Periódico revisado por pares]

United States: Public Library of Science

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Structural elucidation and functional characterization of the Hyaloperonospora arabidopsidis effector protein ATR13
Autor: Leonelli, Lauriebeth ; Pelton, Jeffery ; Schoeffler, Allyn ; Dahlbeck, Douglas ; Berger, James ; Wemmer, David E ; Staskawicz, Brian
Tyler, Brett
Assuntos: Agriculture ; Amino Acid Sequence ; Apoptosis ; Arabidopsis - parasitology ; Arabidopsis Proteins - metabolism ; Arabidopsis thaliana ; Biology ; Cell Nucleolus - metabolism ; Chemistry ; Crystals ; Experiments ; Genetic aspects ; Genetic diversity ; Genetic engineering ; Health aspects ; Microscopy ; Molecular Sequence Data ; Mutagenesis ; Mutation ; Nuclear Proteins - chemistry ; Nuclear Proteins - genetics ; Nuclear Proteins - metabolism ; Oomycetes - genetics ; Oomycetes - pathogenicity ; Physiological aspects ; Plant diseases ; Protein Structure, Secondary ; Proteins ; Virulence - genetics ; Water molds
É parte de: PLoS pathogens, 2011-12, Vol.7 (12), p.e1002428
Notas: Conceived and designed the experiments: LL JP AS DD JB DEW BJS. Performed the experiments: LL JP AS DD DEW. Analyzed the data: LL JP AS DD JB DEW BJS. Contributed reagents/materials/analysis tools: LL JP AS DD. Wrote the paper: LL JP AS DEW BJS.
Descrição: The oomycete Hyaloperonospora arabidopsidis (Hpa) is the causal agent of downy mildew on the model plant Arabidopsis thaliana and has been adapted as a model system to investigate pathogen virulence strategies and plant disease resistance mechanisms. Recognition of Hpa infection occurs when plant resistance proteins (R-genes) detect the presence or activity of pathogen-derived protein effectors delivered to the plant host. This study examines the Hpa effector ATR13 Emco5 and its recognition by RPP13-Nd, the cognate R-gene that triggers programmed cell death (HR) in the presence of recognized ATR13 variants. Herein, we use NMR to solve the backbone structure of ATR13 Emco5, revealing both a helical domain and a disordered internal loop. Additionally, we use site-directed and random mutagenesis to identify several amino acid residues involved in the recognition response conferred by RPP13-Nd. Using our structure as a scaffold, we map these residues to one of two surface-exposed patches of residues under diversifying selection. Exploring possible roles of the disordered region within the ATR13 structure, we perform domain swapping experiments and identify a peptide sequence involved in nucleolar localization. We conclude that ATR13 is a highly dynamic protein with no clear structural homologues that contains two surface-exposed patches of polymorphism, only one of which is involved in RPP13-Nd recognition specificity.
Editor: United States: Public Library of Science
Idioma: Inglês

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Structural elucidation and functional characterization of the Hyaloperonospora arabidopsidis effector protein ATR13

Leonelli, Lauriebeth ; Pelton, Jeffery ; Schoeffler, Allyn ; Dahlbeck, Douglas ; Berger, James ; Wemmer, David E ; Staskawicz, Brian Tyler, Brett

United States: Public Library of Science

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