Bacterial major vault protein homologs form divergent vault structures

Abstract

Vaults are large, enigmatic macromolecular protein complexes composed of symmetrically arranged major vault protein (MVP) subunits with a wide variety of proposed functions. While MVP is conserved in most eukaryotes, its prevalence in other domains of life has not been well studied. Furthermore, whether bacterial MVP homologs assemble into vaults remains unknown. Here, we identify and examine a subset of bacterial MVP homologs and report cryoEM structures of an intact vault from Corallococcus praedator and a half-vault from a Deltaproteobacteria bacterium. Both bacterial vault complexes exhibit architectures unlike any other previously characterized vault with barrel/cap symmetries of D35/C13 and C48/C16, respectively. These data demonstrate that bacterial MVP homologs can assemble into vault structures and highlight the structural diversity of vaults across domains of life.

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BibTeX RIS

BibTeX

@misc{lachowicz2026bacterial,
  title = {{Bacterial major vault protein homologs form divergent vault structures}},
  author = {J. C. Lachowicz and M. Hoque and A. Zhou and T. Zhang and M. C. Franklin and R. Copin and K. D. Cygnar and A. J. Murphy and K. Saotome and A. D. Baik},
  howpublished = {bioRxiv},
  year = {2026},
  month = nov,
  doi = {10.64898/2026.11.06.764734},
  url = {https://www.biorxiv.org/content/10.64898/2026.11.06.764734v1},
  note = {CC BY-NC},
}

RIS

TY  - UNPB
TI  - Bacterial major vault protein homologs form divergent vault structures
AU  - J. C. Lachowicz
AU  - M. Hoque
AU  - A. Zhou
AU  - T. Zhang
AU  - M. C. Franklin
AU  - R. Copin
AU  - K. D. Cygnar
AU  - A. J. Murphy
AU  - K. Saotome
AU  - A. D. Baik
PY  - 2026
DA  - 2026/11/06
PB  - bioRxiv
DO  - 10.64898/2026.11.06.764734
UR  - https://www.biorxiv.org/content/10.64898/2026.11.06.764734v1
AB  - Vaults are large, enigmatic macromolecular protein complexes composed of symmetrically arranged major vault protein (MVP) subunits with a wide variety of proposed functions. While MVP is conserved in most eukaryotes, its prevalence in other domains of life has not been well studied. Furthermore, whether bacterial MVP homologs assemble into vaults remains unknown. Here, we identify and examine a subset of bacterial MVP homologs and report cryoEM structures of an intact vault from Corallococcus praedator and a half-vault from a Deltaproteobacteria bacterium. Both bacterial vault complexes exhibit architectures unlike any other previously characterized vault with barrel/cap symmetries of D35/C13 and C48/C16, respectively. These data demonstrate that bacterial MVP homologs can assemble into vault structures and highlight the structural diversity of vaults across domains of life.
ER  -

Abstract

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