After all that, i just want to thank all the amazing co-authors but particularly @ainsley-beaton.bsky.social for helping me get to the bottom of this story, and my PhD supervisor @matthutchings.bsky.social for always believing in the project!

This leads to the activation of HtrA-family dual function chaperone/proteases that can act to restore the cell to homeostasis! To our knowledge, this is the first proposal of a sensing model for a bacterial secretion or envelope stress response system! (6/7)

Finally, through ChIP-seq, TMT-proteomics and qRT-PCR we managed to link it all. Together with CssRS, CutRS detect secretion stress through the formation (or lack thereof) of the conserved disulfide bond in their sensor kinase sensor domain. (5/n)

Finally, with the help of the amazing @ainsley-beaton.bsky.social, we had a breakthrough. Using a combination of modelling and phylogenetics we discovered that the CutS sensor kinase had a highly conserved dual cysteine motif in its extracellular sensor domain, suddenly we had some clues! (4/n)

My favourite piece of data in the whole paper came after we quantified the biomass difference between the WT and ∆cutRS mutant on glucose media, showing it is around 4x more massive. It also uses up all the glucose in the plate, close to gram, in just 9 days! (3/n)

This mutant also overproduced the antibiotic chloramphenicol, leading to a very potent anti-Gram-postitive activity on plate assays. However, this still didn't give us any clues as to what linked CutRS to the phenotype. (2/n)

Wooo congrats!!

Yes Miguel!!! Huge congrats that’s amazing news! 🎉🎉🎉

Fantastic work Trevor!