Chapter title |
Affinity Purification of Protein Complexes from Drosophila Embryos in Cell Cycle Studies.
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Chapter number | 33 |
Book title |
Cell Cycle Control
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Published in |
Methods in molecular biology, May 2014
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DOI | 10.1007/978-1-4939-0888-2_33 |
Pubmed ID | |
Book ISBNs |
978-1-4939-0887-5, 978-1-4939-0888-2
|
Authors |
Zoltan Lipinszki, Peng Wang, Rhys Grant, Catherine Lindon, Nikola S Dzhindzhev, Pier Paolo D'Avino, Marcin R Przewloka, David M Glover, Vincent Archambault, Lipinszki Z, Wang P, Grant R, Lindon C, Dzhindzhev NS, D'Avino PP, Przewloka MR, Glover DM, Archambault V, Lipinszki, Zoltan, Wang, Peng, Grant, Rhys, Lindon, Catherine, Dzhindzhev, Nikola S., D’Avino, Pier Paolo, Przewloka, Marcin R., Glover, David M., Archambault, Vincent, Nikola S. Dzhindzhev, Pier Paolo D’Avino, Marcin R. Przewloka, David M. Glover |
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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