Post-graduate researcher in the Carella lab! Mad about moss and the evolution of plant immunity 🌱
(they/them)
Elenor Kennedy
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2. Some TIR domains can function independently of both EDS1 and catalytic activity, pointing toward possible alternative signalling mechanisms.
3. Protein architecture matters: expressing TIRs in different protein contexts can alter their mechanism. Worth keeping in mind!
So what does this mean?
1. Many non-seed plant TIR domains can signal through EDS1 in N. benthamiana, even though their native lineages lack EDS1...
We investigated the EDS1-dependence of TIR domains from across the spectrum of land plant evolution, and found that TIR-NLR architecture itself can influence TIR domain activity, even for animal and bacterial TIRs.
We then extended this approach to animal and bacterial TIR domains.
Remarkably, the chimeric TIR-NLR architecture was even sufficient to impose EDS1-dependence on a bacterial TIR domain! 🧫
In seed plants, TIR-NLR immune receptors rely on TIR NADase activity to produce small signalling molecules that are perceived by EDS1 to trigger immunity. However, non-seed plants lack EDS1, raising the question: how do their TIR domains function? 🤔
To investigate this, we expressed TIR-eYFP fusions from across land plant evolution in WT and eds1 N. benthamiana 🌱
Most TIRs were EDS1-dependent. However, some moss and Ginkgo TIR domains functioned independently of both EDS1 and conserved catalytic residues, suggesting alternative mechanisms.
@khongsamchia.bsky.social
Extremely excited to share the first pre-print from my PhD project in the Carella lab, co-first authored with @khongsamchia.bsky.social 🎉 (Thread below ⬇️)
www.biorxiv.org/content/10.6...
Huge thanks to all co-authors and the #CarellaCapybaras for all the support 😊
Surprisingly, when we expressed these same TIR domains on a chimeric TIR-NLR scaffold, they reverted to EDS1-dependence.
This suggests that TIR domain mechanism can be influenced by protein architecture.
