Journal
NATURE
Volume 608, Issue 7922, Pages 429-+Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41586-022-05013-4
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Funding
- UCSD
- National Institutes of Health [R01GM129245, R35 GM144121, R01GM031749, R01-GM129325]
- National Science Foundation [CHE 060073, DBI 1920374]
- Life Sciences Research Foundation
- National Science Foundation Graduate Research Fellowship [DGE-1650112]
- Office of Cyber Infrastructure and Computational Biology, National Institute of Allergy and Infectious Diseases
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This study identifies a protein called ChmA as the main component of the bacteriophage nuclear shell. The structure and dynamics of the ChmA shell provide insights into its formation and functions.
Bacteria encode myriad defences that target the genomes of infecting bacteriophage, including restriction-modification and CRISPR-Cas systems(1). In response, one family of large bacteriophages uses a nucleus-like compartment to protect its replicating genomes by excluding host defence factors(2-4). However, the principal composition and structure of this compartment remain unknown. Here we find that the bacteriophage nuclear shell assembles primarily from one protein, which we name chimallin (ChmA). Combining cryo-electron tomography of nuclear shells in bacteriophage-infected cells and cryo-electron microscopy of a minimal chimallin compartment in vitro, we show that chimallin self-assembles as a flexible sheet into closed micrometre-scale compartments. The architecture and assembly dynamics of the chimallin shell suggest mechanisms for its nucleation and growth, and its role as a scaffold for phage-encoded factors mediating macromolecular transport, cytoskeletal interactions, and viral maturation.
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