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Identification of the bacteriophage nucleus protein interaction network.

Eray EnustunAmar DeepYajie GuKatrina T NguyenVorrapon ChaikeeratisakEmily G ArmbrusterMajid GhassemianElizabeth VillaJoe PoglianoKevin D Corbett
Published in: Nature structural & molecular biology (2023)
In the arms race between bacteria and bacteriophages (phages), some large-genome jumbo phages have evolved a protein shell that encloses their replicating genome to protect it against host immune factors. By segregating the genome from the host cytoplasm, however, the 'phage nucleus' introduces the need to specifically translocate messenger RNA and proteins through the nuclear shell and to dock capsids on the shell for genome packaging. Here, we use proximity labeling and localization mapping to systematically identify proteins associated with the major nuclear shell protein chimallin (ChmA) and other distinctive structures assembled by these phages. We identify six uncharacterized nuclear-shell-associated proteins, one of which directly interacts with self-assembled ChmA. The structure and protein-protein interaction network of this protein, which we term ChmB, suggest that it forms pores in the ChmA lattice that serve as docking sites for capsid genome packaging and may also participate in messenger RNA and/or protein translocation.
Keyphrases
  • protein protein
  • small molecule
  • genome wide
  • binding protein
  • amino acid
  • high resolution
  • gene expression
  • preterm infants
  • molecular dynamics
  • pseudomonas aeruginosa
  • molecular dynamics simulations