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    In vivo protein trapping produces a functional expression codex of the vertebrate proteome

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    Name:
    In vivo protein trapping produces ...
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    Genre
    Journal Article
    Date
    2011-06-01
    Author
    Clark, KJ
    Balciunas, D
    Pogoda, HM
    Ding, Y
    Westcot, SE
    Bedell, VM
    Greenwood, TM
    Urban, MD
    Skuster, KJ
    Petzold, AM
    Ni, J
    Nielsen, AL
    Patowary, A
    Scaria, V
    Sivasubbu, S
    Xu, X
    Hammerschmidt, M
    Ekker, SC
    Show allShow less
    Subject
    Animals
    Animals, Genetically Modified
    DNA Transposable Elements
    Gene Expression Profiling
    Gene Knockdown Techniques
    Models, Animal
    Molecular Sequence Data
    Mutagenesis, Insertional
    Proteome
    Proteomics
    Zebrafish
    Zebrafish Proteins
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    Permanent link to this record
    http://hdl.handle.net/20.500.12613/6038
    
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    DOI
    10.1038/nmeth.1606
    Abstract
    We describe a conditional in vivo protein-trap mutagenesis system that reveals spatiotemporal protein expression dynamics and can be used to assess gene function in the vertebrate Danio rerio. Integration of pGBT-RP2.1 (RP2), a gene-breaking transposon containing a protein trap, efficiently disrupts gene expression with >97% knockdown of normal transcript amounts and simultaneously reports protein expression for each locus. The mutant alleles are revertible in somatic tissues via Cre recombinase or splice-site-blocking morpholinos and are thus to our knowledge the first systematic conditional mutant alleles outside the mouse model. We report a collection of 350 zebrafish lines that include diverse molecular loci. RP2 integrations reveal the complexity of genomic architecture and gene function in a living organism and can provide information on protein subcellular localization. The RP2 mutagenesis system is a step toward a unified 'codex' of protein expression and direct functional annotation of the vertebrate genome. © 2011 Nature America, Inc. All rights reserved.
    Citation to related work
    Springer Science and Business Media LLC
    Has part
    Nature Methods
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    ae974a485f413a2113503eed53cd6c53
    http://dx.doi.org/10.34944/dspace/6020
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