It was a lovely week in Seoul! Now going back home, with wonderful memories of my favorite places in Seoul and of course all the amazing food!

It was an incredible honor to be invited and introduce my work at the 34th International Korean Genome Organization conference! I learned so much about genomes in multiple model systems and about all the fascinating works done by Korean genomics experts! #KOGO

Ahn Lab is going to MPMI! #2025ISMPMI
Hayden Burdett and myself will be attending the MPMI conference in Cologne ⛪
Check out poster P-073 for paired NLR biology, and let's chat about paired NLRs and more!🌱
See you in Cologne 😀
@instmolplantsci.bsky.social

Beautiful talk by @kmerchante.bsky.social at #TLUK25 today! Ribosome heterogeneity in plants is so so interesting! @biochemsoc.bsky.social

@instmolplantsci.bsky.social very own Amy Newell presents her work on shade response in plants and translational regulation at the #TLUK25!! @biochemsoc.bsky.social

Wonderful talk by Baptiste Castel @baptistebio.bsky.social on fern immune system here at @instmolplantsci.bsky.social Great to meet @jonathandgjones.bsky.social lab alumni in Edinburgh too!

Finally, what is the evolutionary advantage of having these complexes? If the immune receptors are already close together, or even better, already forming a complex and need just a little transformation, response to pathogens will be much faster. (15/)

We measured the NADase activity from RRS1-R/RPS4 complex purified from plants, and NADase activity was only observed from active complexes including RRS1-R. This suggests that RRS1-R also has a role in the activated complex. (11/)

Next, we tested whether RRS1-R/RPS4 complex changes oligomeric states upon pathogen recognition. But we didn’t see any change. We had predicted that maybe RRS1-R may dissociate from the complex because it doesn’t have any NAD+ hydrolysis activity, but that was not the case. (10/)

Next, we wanted to identify the domains important for this protein complex assembly. We showed that the interaction interface of the foremost TIR domain is essential for forming the RRS1-R/RPS4 complex. Mutating the enzymatic function had no effect on complex association. (7/)