Thank you! I'd love to swing by your lab and chat sometime.

Thanks, there is so much more to explore!

Many thanks to our wonderful collaborators and to the Gao lab to make this work possible!

Our findings reveal an incredible diversity of protease-based regulatory strategies that can respond to diverse phage stimuli.

4. EACC1, another small hypothetical protein, assembles into a toxic membrane pore after proteolytic removal of its N-terminal auto-inhibitory domain. Surprisingly, some EACC1-protease pairs are fused to divergent Dnak-like chaperones.

3. The small hypothetical protein, Pepco, pre-assembles into a β-barrel oligomer that is toxic after cleavage of 2kDa C-terminal fragments. Pepco oligomers are remarkably stable, surviving detergent and heat.

2. A toxic α/β-hydrolase is activated by proteolytic removal at two distinct internal sites and requires two of the three fragments for cellular toxicity.

1. A toxic zinc-dependent nuclease with an MBL fold is activated by proteolytic cleavage of two auto-inhibitory linkers and requires all three fragments for cellular toxicity.

These findings support fantastic work by @owentuck.bsky.social and the @doudna-lab.bsky.social!