The Structure of Rat Liver Vault at 3.5 Angstrom Resolution

@article{Tanaka2009TheSO,
  title={The Structure of Rat Liver Vault at 3.5 Angstrom Resolution},
  author={Hideaki Tanaka and Koji Kato and Eiki Yamashita and Tomoyuki Sumizawa and Yong Zhou and Min Yao and Kenji Iwasaki and Masato Yoshimura and Tomitake Tsukihara},
  journal={Science},
  year={2009},
  volume={323},
  pages={384 - 388}
}
Vaults are among the largest cytoplasmic ribonucleoprotein particles and are found in numerous eukaryotic species. Roles in multidrug resistance and innate immunity have been suggested, but the cellular function remains unclear. We have determined the x-ray structure of rat liver vault at 3.5 angstrom resolution and show that the cage structure consists of a dimer of half-vaults, with each half-vault comprising 39 identical major vault protein (MVP) chains. Each MVP monomer folds into 12… 
Structural studies of large nucleoprotein particles, vaults
Vault is the largest nonicosahedral cytosolic nucleoprotein particle ever described. The widespread presence and evolutionary conservation of vaults suggest important biologic roles, although their
X-ray Crystal Structure of the Vault, Largest Ribonucleoprotein Particle, with a Molecular Weight of 10 MDa
TLDR
The X-ray structure of rat liver vault is determined at 3.5 A resolution and it is shown that the shoulder domain of MVP is structurally similar to SPFH (stomatin/prohibitin/flotillin/HflK/C) domain involved in lipid raft association.
Structural Dynamics of the Vault Ribonucleoprotein Particle
TLDR
The high resolution, crystal structure of the of the seven N-terminal domains of MVP, forming the central vault barrel, revealed the interactions governing vault association and suggested a pH-dependent mechanism for a reversible dissociation induced by low pH.
The mechanism of vault opening from the high resolution structure of the N-terminal repeats of MVP
TLDR
The crystal structure of the vault particle solved at 8 Å resolution, together with the 7 N‐terminal domains of MVP, reveal the interactions governing vault association and provide an explanation for a reversible dissociation induced by low pH.
MVP and vaults: a role in the radiation response
TLDR
New roles have been assigned to MVP and vaults including the association with the insulin-like growth factor-1, hypoxia-induciblefactor-1alpha, and the two major DNA double-strand break repair machineries: non-homologous endjoining and homologous recombination.
Solution Structures of Engineered Vault Particles
Prior crystal structures of the vault have provided clues of its structural variability but are non-conclusive due to crystal packing. Here, we obtained vaults by engineering at the N-terminus of rat
In Silico Resurrection of the Major Vault Protein Suggests It Is Ancestral in Modern Eukaryotes
TLDR
The conclusion from the distribution of vaults is that they were present in the last eukaryote common ancestor but they have apparently been lost from a number of groups including fungi, insects, and probably plants.
Modulation of the Vault Protein-Protein Interaction for Tuning of Molecular Release
TLDR
The interactions between the isolated INT-interacting MVP domains (iMVP) and wild-type INT and compared them to two structurally modified INT: 15-amino acid deletion at the C terminus (INTΔC15) and histidine substituted at the interaction surface (INT/DSA/3 H) to impart a pH-sensitive response.
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References

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Draft Crystal Structure of the Vault Shell at 9-Å Resolution
Vaults are the largest known cytoplasmic ribonucleoprotein structures and may function in innate immunity. The vault shell self-assembles from 96 copies of major vault protein and encapsulates two
RNA location and modeling of a WD40 repeat domain within the vault.
TLDR
To locate the position of the vRNA, vaults were treated with RNases, and cryo-electron microscopy was performed on the resulting complexes, revealing the v RNA to be at the ends of the vault caps.
Vaults. III. Vault ribonucleoprotein particles open into flower-like structures with octagonal symmetry
TLDR
A structural model is proposed that predicts the stoichiometry of vault proteins and RNA, defines vault dimer-monomer interactions, and describes two possible modes for unfolding of vaults into flowers, likely to play a role in vault function.
Assembly of Vault-like Particles in Insect Cells Expressing Only the Major Vault Protein*
TLDR
These particles are the first example of a single protein polymerizing into a non-spherically, non-cylindrically symmetrical structure and will enable us to design agents that disrupt vault formation and aid in elucidating vault functionin vivo.
Vaults. II. Ribonucleoprotein structures are highly conserved among higher and lower eukaryotes
TLDR
The isolation of vaults from numerous species is reported and it is shown that vaults appear to be ubiquitous among eukaryotes, including mammals, amphibians and Xenopus laevis, avians, and the lower Eukaryote Dictyostelium discoideum.
Evidence that vault ribonucleoprotein particles localize to the nuclear pore complex.
TLDR
The present study demonstrates that vaults specifically associate with nuclei by both immunoblotting and immunofluorescence, and confirmed that vault associate with the nuclear envelope in tissue sections and with NPCs of isolated nuclei.
The 193-Kd Vault Protein, Vparp, Is a Novel Poly(Adp-Ribose) Polymerase
TLDR
The 193-kD vault protein is identified by its interaction with the MVP in a yeast two-hybrid screen and confirmed its identity by peptide sequence analysis, and it is shown that one substrate for this vault-associated PARP activity is the MVP.
Vaults and Telomerase Share a Common Subunit, TEP1*
TLDR
It is shown that while TEP1 is a component of the vault particle, vaults have no detectable telomerase activity, suggesting that TEP 1 may play a common role in some aspect of ribonucleoprotein structure, function, or assembly.
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