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PreprintCited by 32Bacteriophages and microbial interactionsCRISPR and Genetic EngineeringBacterial Genetics and Biotechnology

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Bacterial Shedu immune nucleases share a common enzymatic core regulated by diverse sensor domains

Open access
Gu, Yajie, Li, Huan, Deep, Amar, Enustun, Eray, Zhang, Dapeng, Corbett, Kevin D.·2023·Molecular Cell
DOI 10.1101/2023.08.10.552793PMC PMC11805627

Preprint — published as 10.1016/j.molcel.2024.12.004 · Paper page

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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.

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Metadata

Authors
Gu, Y., Li, H., Deep, A., Enustun, E., Zhang, D., & Corbett, K. D.
Affiliations
  • University of California San Diego (US)
  • Saint Louis University (US)
Corresponding author
  • Zhang, Dapeng
  • Corbett, Kevin D.
ORCID
Venue
Molecular Cell
Publisher
openRxiv
Published
2023-08-10
Volume
85
Issue
3
Pages
523-536.e6
ISSN
1097-2765 (ISSN-L)
DOI
10.1101/2023.08.10.552793
PMC
PMC11805627
OpenAlex
W4405924992
Cited by
32
References
1
Citations by year
2026: 13 · 2025: 12 · 2024: 7
FWCI
8.75
Type
journal article
Language
en
Open access
Locations
  • Molecular Cell (publishedVersion)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
  • PubMed Central (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (submittedVersion, cc-by-nc-nd)
Funders
  • Howard Hughes Medical Institute
  • Saint Louis University
  • National Institutes of Health
  • University of California, San Diego
  • National Institute of General Medical Sciences (R35GM144121)
Topics
  • Life Sciences › Immunology and Microbiology › Virology › Bacteriophages and microbial interactions
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › CRISPR and Genetic Engineering
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Keywords
Bacillus cereus, nuclease activation, conformational change, N-terminal domain, sensor domain, cryo-EM structure

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