Vaults. III. Vault ribonucleoprotein particles open into flower-like structures with octagonal symmetry.

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Vaults. III. Vault ribonucleoprotein particles open into flower-like structures with octagonal symmetry

The structure of rat liver vault ribonucleoprotein particles was examined using several different staining techniques in conjunction with EM and digestion with hydrolytic enzymes. Quantitative scanning transmission EM demonstrates that each vault particle has a total mass of 12.9 +/- 1 MD and contains two centers of mass, suggesting that each vault particle is a dimer. Freeze-etch reveals that ...

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The structure of the ribonucleoprotein (RNP) complex of three coronaviruses was investigated. A single-stranded helix of diam. 14 to 16 nm and up to 320 nm in length was released from disrupted particles of human coronavirus strain 229E and mouse hepatitis virus strain 3 after incubation in mild conditions. The helical complexes appeared to be composed of globular subunits with long axes of 5 t...

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Investigating Antibody Access to Adsorbed Protein Nanocapsule Interiors Using the Quartz Crystal Microbalance and Surface Plasmon Resonance

Vaults are nanoscale, ribonucleoprotein capsules (41 nm × 41 nm × 72.5 nm [1]) comprised primarily of 96 self-assembled copies of one 96 kDa protein, termed MVP (major vault protein). When deposited on polylysine-coated mica and imaged using cryoelectron microscopy, vaults appear to “open” into flower-like structures with eight rectangular ‘petals’ [2]. Upon closer examination, each ‘flower’ co...

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A vault ribonucleoprotein particle exhibiting 39-fold dihedral symmetry

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) polyme...

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A vault ribonucleoprotein particle exhibiting 39-fold dihedral symmetry. Corrigendum

Insutitute for Protein Research, Osaka University, 3-2 Yamada-oka, Suita 565-0871, Japan, Department of Environmental Toxicology, Institute of Industrial Ecological Sciences, University of Occupational and Environmental Health, 1-1 Iseigaoka, Yahatanishi, Kitakyushu 807-8555, Japan, Bio-multisome Research Team, Structural Physiology Research Group, RIKEN Harima Institute, Mikazuki Sayo, Hyogo 6...

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ژورنال

عنوان ژورنال: Journal of Cell Biology

سال: 1991

ISSN: 0021-9525,1540-8140

DOI: 10.1083/jcb.112.2.225