ORCID Profile
0000-0002-5417-6963
Current Organisation
Australian National University
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Research Topics
In Research Link Australia (RLA), "Research Topics" refer to ANZSRC FOR and SEO codes. These topics are either sourced from ANZSRC FOR and SEO codes listed in researchers' related grants or generated by a large language model (LLM) based on their publications.
Top 5 Research Topics
ANZSRC Field of Research (FoR)
Plant Cell and Molecular Biology | Biochemistry and Cell Biology | Structural Biology (incl. Macromolecular Modelling) | Synthetic Biology |
ANZSRC Socio-Economic Objective (SEO)
Control of Plant Pests, Diseases and Exotic Species in Farmland, Arable Cropland and Permanent Cropland Environments | Expanding Knowledge in the Biological Sciences | Wheat
Related Links
Publications
Loss of AvrSr50 by somatic exchange in stem rust leads to virulence for Sr50 resistance in wheat
Publisher: American Association for the Advancement of Science (AAAS)
Date: 22-12-2017
Abstract: The fungal pathogen Ug99 (named for its identification in Uganda in 1999) threatens wheat crops worldwide. Ug99 can kill entire fields of wheat and is undeterred by many of the disease-resistance genes that otherwise protect wheat crops. Two papers describe two peptides secreted by the fungus as it attacks the wheat (see the Perspective by Moscou and van Esse). Chen et al. show that fungal AvrSr50 binds to the plant's immune receptor Sr50, and Salcedo et al. show that fungal AvrSr35 binds to Sr35. Successful binding activates the plant's immune defenses. Removing or inactivating these Avr effectors leaves the plant defenseless and susceptible to disease. Science , this issue p. 1607 , p. 1604 see also p. 1541
Nagasaki: life after nuclear war
Publisher: Informa UK Limited
Date: 15-08-2016
Silences: The Catholics, the Untouchables and the Nagasaki Atomic Bomb
Publisher: Informa UK Limited
Date: 09-12-2020
Multiple functional self-association interfaces in plant TIR domains
Publisher: Proceedings of the National Academy of Sciences
Date: 03-02-2017
Abstract: Toll/interleukin-1 receptor/resistance protein (TIR) domains are present in plant and animal innate immunity receptors and appear to play a scaffold function in defense signaling. In both systems, self-association of TIR domains is crucial for their function. In plants, the TIR domain is associated with intracellular immunity receptors, known as nucleotide-binding oligomerization domain-like receptors (NLRs). Previous studies from several plant NLRs have identified two distinct interfaces that are required for TIR:TIR dimerization in different NLRs. We show that the two interfaces previously identified are both important for self-association and defense signaling of multiple TIR–NLR proteins. Collectively, this work suggests that there is a common mechanism of TIR domain self-association in signaling across the TIR–NLR class of receptor proteins.
What Do We Know About NOD-Like Receptors in Plant Immunity?
Publisher: Annual Reviews
Date: 04-08-2017
DOI: 10.1146/ANNUREV-PHYTO-080516-035250
Abstract: The first plant disease resistance (R) genes were identified and cloned more than two decades ago. Since then, many more R genes have been identified and characterized in numerous plant pathosystems. Most of these encode members of the large family of intracellular NLRs (NOD-like receptors), which also includes animal immune receptors. New discoveries in this expanding field of research provide new elements for our understanding of plant NLR function. But what do we know about plant NLR function today? Genetic, structural, and functional analyses have uncovered a number of commonalities and differences in pathogen recognition strategies as well as how NLRs are regulated and activate defense signaling, but many unknowns remain. This review gives an update on the latest discoveries and breakthroughs in this field, with an emphasis on structural findings and some comparison to animal NLRs, which can provide additional insights and paradigms in plant NLR function.
Induced proximity of a TIR signaling domain on a plant-mammalian NLR chimera activates defense in plants.
Publisher: Proceedings of the National Academy of Sciences
Date: 24-07-2020
Abstract: Animal NLRs form wheel-like structures called inflammasomes upon perception of pathogen-associated molecules. The induced proximity of the signaling domains at the center of the wheel is hypothesized to recruit caspases for the first step of immune signal transduction. We expressed a plant-animal NLR fusion to demonstrate that induced proximity of TIR signaling domains from plant NLRs is sufficient to activate plant immune signaling. This demonstrates that a signaling-competent inflammasome can be formed from known, minimal components. The intrinsic NADase activity of plant TIRs is necessary for immune signaling, but fusions to a bacterial or a mammalian TIR domain with NADase activity, which also lead to accumulation of NAD + hydrolysis products (e.g. cyclic ADP-ribose), were unable to activate immune signaling.
Production of small cysteine‐rich effector proteins in Escherichia coli for structural and functional studies
Publisher: Wiley
Date: 12-04-2016
DOI: 10.1111/MPP.12385
Dangerous Memory in Nagasaki Prayers: Protests and Catholic Survivor Narratives
Publisher: Routledge
Date: 10-09-2020
Japan: History and Culture from Classical to Cool
Publisher: The Japan Foundation, Sydney
Date: 07-2019
Direct recognition of effectors by plant NLR immune receptors and downstream signalling
Publisher: Portland Press Ltd.
Date: 09-2022
DOI: 10.1042/EBC20210072
Abstract: Plants deploy extracellular and intracellular immune receptors to sense and restrict pathogen attacks. Rapidly evolving pathogen effectors play crucial roles in suppressing plant immunity but are also monitored by intracellular nucleotide-binding, leucine-rich repeat immune receptors (NLRs), leading to effector-triggered immunity (ETI). Here, we review how NLRs recognize effectors with a focus on direct interactions and summarize recent research findings on the signalling functions of NLRs. Coiled-coil (CC)-type NLR proteins execute immune responses by oligomerizing to form membrane-penetrating ion channels after effector recognition. Some CC-NLRs function in sensor–helper networks with the sensor NLR triggering oligomerization of the helper NLR. Toll/interleukin-1 receptor (TIR)-type NLR proteins possess catalytic activities that are activated upon effector recognition-induced oligomerization. Small molecules produced by TIR activity are detected by additional signalling partners of the EDS1 lipase-like family (enhanced disease susceptibility 1), leading to activation of helper NLRs that trigger the defense response.
NAD + cleavage activity by animal and plant TIR domains in cell death pathways
Publisher: American Association for the Advancement of Science (AAAS)
Date: 23-08-2019
Abstract: One way that plants respond to pathogen infection is by sacrificing the infected cells. The nucleotide-binding leucine-rich repeat immune receptors responsible for this hypersensitive response carry Toll/interleukin-1 receptor (TIR) domains. In two papers, Horsefield et al. and Wan et al. report that these TIR domains cleave the metabolic cofactor nicotinamide adenine dinucleotide (NAD + ) as part of their cell-death signaling in response to pathogens. Similar signaling links mammalian TIR-containing proteins to NAD + depletion during Wallerian degeneration of neurons. Science , this issue p. 793 , p. 799
Crystallization and preliminary X-ray diffraction analyses of the TIR domains of three TIR-NB-LRR proteins that are involved in disease resistance in Arabidopsis thaliana.
Publisher: International Union of Crystallography (IUCr)
Date: 30-10-2013
Crystal structure of the Melampsora lini effector AvrP reveals insights into a possible nuclear function and recognition by the flax disease resistance protein P
Publisher: Wiley
Date: 16-11-2017
DOI: 10.1111/MPP.12597
Faking Liberties: Religious Freedom in American-Occupied Japan. By Jolyon Baraka Thomas
Publisher: Oxford University Press (OUP)
Date: 2020
DOI: 10.1093/JCS/CSAA020
Subcellular localization requirements and specificities for plant immune receptor Toll‐interleukin‐1 receptor signaling
Publisher: Wiley
Date: 03-04-2023
DOI: 10.1111/TPJ.16195
Abstract: Recent work shed light on how plant intracellular immune receptors of the nucleotide‐binding leucine‐rich repeat (NLR) family are activated upon pathogen effector recognition to trigger immune responses. Activation of Toll‐interleukin‐1 receptor (TIR) domain‐containing NLRs (TNLs) induces receptor oligomerization and close proximity of the TIR domain, which is required for TIR enzymatic activity. TIR‐catalyzed small signaling molecules bind to EDS1 family heterodimers and subsequently activate downstream helper NLRs, which function as Ca 2+ permeable channel to activate immune responses eventually leading to cell death. Subcellular localization requirements of TNLs and signaling partners are not well understood, although they are required to understand fully the mechanisms underlying NLR early signaling. TNLs show erse subcellular localization while EDS1 shows nucleocytosolic localization. Here, we studied the impact of TIR and EDS1 mislocalization on the signaling activation of different TNLs. In Nicotiana benthamiana , our results suggest that close proximity of TIR domains isolated from flax L6 and Arabidopsis RPS4 and SNC1 TNLs drives signaling activation from different cell compartments. Nevertheless, both Golgi‐membrane anchored L6 and nucleocytosolic RPS4 have the same requirements for EDS1 subcellular localization in Arabidopsis thaliana . By using mislocalized variants of EDS1, we found that autoimmune L6 and RPS4 TIR domain can induce seedling cell death when EDS1 is present in the cytosol. However, when EDS1 is restricted to the nucleus, both induce a stunting phenotype but no cell death. Our data point out the importance of thoroughly investigating the dynamics of TNLs and signaling partners subcellular localization to understand TNL signaling fully.
Crystallization and preliminary X-ray diffraction analysis of the flax cytokinin oxidase LuCKX1.1
Publisher: International Union of Crystallography (IUCr)
Date: 28-09-2013
Mary, Mothers, Lament, and Feminist Theology
Publisher: Indiana University Press
Date: 2020
Oral History and Australian Generations. Katie Holmes and Alistair Thomson (eds.). London: Routledge, 2017. 122 pp. ISBN 978-0-4157-88953 (Hardbound) $170.00; ISBN 978-0-3671-33627 (Softbound) $49.95; ISBN 978-1-31522-3063 (E-book) $24.98
Publisher: Informa UK Limited
Date: 23-11-2021
Comparative Analysis of the Flax Immune Receptors L6 and L7 Suggests an Equilibrium-Based Switch Activation Model
Publisher: Oxford University Press (OUP)
Date: 2016
DOI: 10.1105/TPC.15.00303
Structural Basis for Assembly and Function of a Heterodimeric Plant Immune Receptor
Publisher: American Association for the Advancement of Science (AAAS)
Date: 18-04-2014
Abstract: Certain pathogen effectors are detected in plants by cytoplasmic receptors. First solving the crystal structures of Arabidopsis receptors, Williams et al. (p. 299 see the Perspective by Nishimura and Dangl ) discovered that in the resting state, the structures form a heterodimer that readies the complex for effector binding and keeps the signaling domains from firing too early. Once the pathogen effector binds, the structure of the complex shifts such that the signaling domains can form a homodimer to initiate downstream signaling. Similarities between these plant-pathogen receptors and Toll-like receptors in animals suggest the molecular mechanisms may translate broadly.
Structural and functional analysis of a plant resistance protein TIR domain reveals interfaces for self-association, signaling, and autoregulation.
Publisher: Elsevier BV
Date: 03-2011
Related Organisations
Commonwealth Scientific And Industrial Research Organisation (CSIRO)
Location: Australia
Related Funding Activities
Discovery Early Career Researcher Award - Grant ID: DE210100323
Start Date: 01-2021
End Date: 12-2024
Amount: $431,000.00
Funder: Australian Research Council
View Funded Activity