Architecture and self-assembly of the jumbo bacteriophage nuclear shell

Article

关键词: MOLECULAR-DYNAMICS SIMULATIONS;    PARTICLE CRYO-EM;    BAYESIAN-APPROACH;    MODEL;    REFINEMENT;    PROTEINS;    ROBUST;    PHAGE;    IMPLEMENTATION;    PSEUDOMONAS;   

DOI  :  10.1038/s41586-022-05013-4

来源: SCIE

【 摘 要 】

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.

【 授权许可】

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