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    In silico resurrection of the major vault protein suggests it is ancestral in modern eukaryotes

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    In silico resurrection of the major vault protein suggests it is ancestral in modern eukaryotes.pdf (1.574Mb)
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    10.1093/gbe/evt113
     
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    Abstract
    Vaults are very large oligomeric ribonucleoproteins conserved among a variety of species. The rat vault 3D structure shows an ovoid oligomeric particle, consisting of 78 major vault protein monomers, each of approximately 861 amino acids. Vaults are probably the largest ribonucleoprotein structures in eukaryote cells, being approximately 70 nm in length with a diameter of 40 nm--the size of three ribosomes and with a lumen capacity of 50 million Å(3). We use both protein sequences and inferred ancestral sequences for in silico virtual resurrection of tertiary and quaternary structures to search for vaults in a wide variety of eukaryotes. We find that the vault's phylogenetic distribution is widespread in eukaryotes, but is apparently absent in some notable model organisms. Our 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. Our approach of inferring ancestral 3D and quaternary structures is expected to be useful generally.
    Citation
    GENOME BIOLOGY AND EVOLUTION, 2013, 5 (8), pp. 1567 - 1583 (17)
    Date
    2013-07-25
    Author
    Daly TK
    Sutherland-Smith AJ
    Penny ED
    Rights
    CC BY-NC 3.0
    Publisher
    Oxford University Press
    Description
    (c) The Author(s) 2013
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    DSpace software copyright © Duraspace
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