Abstract
Vault is a 12.9 MDa ribonucleoprotein particle with a barrel-like shape, two protruding caps and an invaginated waist structure that is highly conserved in a wide variety of eukaryotes. Multimerization of the major vault protein (MVP) is sufficient to assemble the entire exterior shell of the barrel-shaped vault particle. Multiple copies of two additional proteins, vault poly(ADP-ribose) polymerase (VPARP) and telomerase-associated protein 1 (TEP1), as well as a small vault RNA (vRNA), are also associated with vault. Here, the crystallization of vault particles is reported. The crystals belong to space group C2, with unit-cell parameters a = 708.0, b = 385.0, c = 602.9 angstroms, beta = 124.8 degrees . Rotational symmetry searches based on the R factor and correlation coefficient from noncrystallographic symmetry (NCS) averaging indicated that the particle has 39-fold dihedral symmetry.
Highlights
Vault is a large ribonucleoprotein particle with a unique barrel-shaped structure that is widely conserved among eukaryotes (Kedersha & Rome, 1986)
Expression of major vault protein (MVP) alone in insect cells leads to the assembly of recombinant MVP-only vault, demonstrating that the multimerization of this single protein is sufficient to form the exterior shell of the vault particle (Stephen et al, 2001)
This led the authors to propose a model of the complex that has eightfold dihedral symmetry and that contains one copy of telomerase-associated protein 1 (TEP1), four copies of vault poly(ADP-ribose) polymerase (VPARP) and three or more copies of vault RNA (vRNA) in each cap
Summary
Vault is a large ribonucleoprotein particle with a unique barrel-shaped structure that is widely conserved among eukaryotes (Kedersha & Rome, 1986). Imposing eightfold symmetry, Kong et al (1999) analyzed the structure of rat vault using a cryoelectronmicroscopic method This revealed the reconstructed structure of the rat vault to be a hollow barrel-like structure with two protruding caps and an invaginated waist; 96 copies of MVP were predicted to form the barrel-shaped core of the particle. Difference mapping between RNase-treated and intact vaults revealed that vRNA is localized at the end of the vault caps (Kong et al, 2000) This led the authors to propose a model of the complex that has eightfold dihedral symmetry (point group D8) and that contains one copy of TEP1, four copies of VPARP and three or more copies of vRNA in each cap. A hanging drop was prepared by mixing equal volumes of vault solution and precipitant solution containing polyethylene glycol (PEG)
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