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Lipinszki, Z., Wang, P., Grant, R., Lindon, C., Dzhindzhev, N.S., D'Avino, P.P., Przewloka, M.R., Glover, D.M., Archambault, V. (2014). Affinity purification of protein complexes from Drosophila embryos in cell cycle studies.  Methods Mol. Biol. 1170(): 571--588.
FlyBase ID
FBrf0225277
Publication Type
Research paper
Abstract
The ability to identify protein interactions is key to elucidating the molecular mechanisms of cellular processes, including mitosis and cell cycle regulation. Drosophila melanogaster, as a model system, provides powerful tools to study cell division using genetics, microscopy, and RNAi. Drosophila early embryos are highly enriched in mitotic protein complexes as their nuclei undergo 13 rounds of rapid, synchronous mitotic nuclear divisions in a syncytium during the first 2 h of development. Here, we describe simple methods for the affinity purification of protein complexes from transgenic fly embryos via protein A- and green fluorescent protein-tags fused to bait proteins of interest. This in vivo proteomics approach has allowed the identification of several known and novel mitotic protein interactions using mass spectrometry, and it expands the use of the Drosophila model in modern molecular biology.
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    Language of Publication
    English
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    Parent Publication
    Publication Type
    Journal
    Abbreviation
    Methods Mol. Biol.
    Title
    Methods in molecular biology (Clifton, N.J.)
    ISBN/ISSN
    1064-3745 1940-6029
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