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Sea urchin vault structure, composition, and differential localization during development

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BioMed Central
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PMC
Keywords
  • Research Article
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  • Biology

Abstract

1471-213X-5-3.fm ral ss BioMed CentBMC Developmental Biology Open AcceResearch article Sea urchin vault structure, composition, and differential localization during development Phoebe L Stewart*1,2, Miriam Makabi2, Jennifer Lang3, Carrie Dickey-Sims4, Anthony J Robertson4, James A Coffman4 and Kathy A Suprenant3 Address: 1Department of Molecular Physiology and Biophysics, Vanderbilt University Medical Center, Nashville, TN USA, 2Department of Molecular and Medical Pharmacology, Crump Institute for Molecular Imaging, David Geffen School of Medicine at UCLA, Los Angeles, CA USA, 3Department of Molecular Biosciences, University of Kansas, Lawrence, KS USA and 4Stowers Institute for Medical Research, Kansas City, MO USA Email: Phoebe L Stewart* - [email protected]; Miriam Makabi - [email protected]; Jennifer Lang - [email protected]; Carrie Dickey-Sims - [email protected]; Anthony J Robertson - [email protected]; James A Coffman - [email protected]; Kathy A Suprenant - [email protected] * Corresponding author Abstract Background: Vaults are intriguing ribonucleoprotein assemblies with an unknown function that are conserved among higher eukaryotes. The Pacific coast sea urchin, Strongylocentrotus purpuratus, is an invertebrate model organism that is evolutionarily closer to humans than Drosophila and C. elegans, neither of which possesses vaults. Here we compare the structures of sea urchin and mammalian vaults and analyze the subcellular distribution of vaults during sea urchin embryogenesis. Results: The sequence of the sea urchin major vault protein (MVP) was assembled from expressed sequence tags and genome traces, and the predicted protein was found to have 64% identity and 81% similarity to rat MVP. Sea urchin MVP includes seven ~50 residue repeats in the N-terminal half of the protein and a predicted coiled coil domain in the C-terminus, as does rat MVP. A cryoelectron microscopy (cryoEM) reconstruction of isolated sea urchin

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