Abstract
Understanding protein–protein interactions and the architecture of protein complexes in which they work is essential to identify their biological role. Protein co-immunoprecipitation (co-IP) is an invaluable technique used in biochemistry allowing the identification of protein interactors. Here, we describe in detail an immunoaffinity purification protocol as a one-step or two-step immunoprecipitation from budding yeast Saccharomyces cerevisiae cells to subsequently detect interactions between proteins involved in the same biological process.
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Acknowledgements
We are grateful for teaching and scientific advice to Professor Karim Labib. Methods described in this chapter were developed in Labib’s laboratory and we would like to thank members of his group past and present who contributed to our current understanding of methods presented here. We especially thank Dr. Frederick van Deursen, Dr. Sugopa Sengupta and Dr. Giacomo De Piccoli for comments on the manuscript. ASD is a recipient of a Ramon y Cajal contract and received funding from the Cantabria International Campus and via grant BFU2011-23193 from the Spanish “Ministerio de Economia y Competitividad” (co-funded by the European Regional Development Fund).
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Foltman, M., Sanchez-Diaz, A. (2016). Studying Protein–Protein Interactions in Budding Yeast Using Co-immunoprecipitation. In: Sanchez-Diaz, A., Perez, P. (eds) Yeast Cytokinesis. Methods in Molecular Biology, vol 1369. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-3145-3_17
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DOI: https://doi.org/10.1007/978-1-4939-3145-3_17
Publisher Name: Humana Press, New York, NY
Print ISBN: 978-1-4939-3144-6
Online ISBN: 978-1-4939-3145-3
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