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- W4385766486 abstract "Summary Prokaryotes encode diverse anti-bacteriophage immune systems, including the single-protein Shedu nuclease. Here we reveal the structural basis for activation of Bacillus cereus Shedu. In the inactive homotetramer, a key catalytic residue in Shedu’s nuclease domain is sequestered away from the catalytic site. Activation involves a conformational change that completes the active site and promotes assembly of a homo-octamer for coordinated double-strand DNA cleavage. Removal of Shedu’s N-terminal domain ectopically activates the enzyme, suggesting that this domain allosterically inhibits Shedu in the absence of infection. Bioinformatic analysis of nearly 8,000 Shedu homologs reveals remarkable diversity in their N-terminal regulatory domains: we identify 79 domain families falling into eight functional classes, including diverse nucleic acid binding, enzymatic, and other domains. Together, these data reveal Shedu as a broad family of immune nucleases with a common nuclease core regulated by diverse N-terminal domains that likely respond to a range of infection-related signals." @default.
- W4385766486 created "2023-08-12" @default.
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- W4385766486 date "2023-08-10" @default.
- W4385766486 modified "2023-09-28" @default.
- W4385766486 title "Bacterial Shedu immune nucleases share a common enzymatic core regulated by diverse sensor domains" @default.
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- W4385766486 doi "https://doi.org/10.1101/2023.08.10.552793" @default.
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