Individual proteins often function as part of a protein complex. The identification of interacting proteins is therefore vital to understand the biological role and function of the studied protein. Here we describe a method for the in vivo identification of nuclear, cytoplasmic, and membrane-associated protein complexes from plant tissues using a strategy of immunoprecipitation followed by tandem mass spectrometry. By performing quantitative mass spectrometry measurements on biological triplicates, relative abundance of proteins in GFP-tagged complexes compared to background controls can be statistically evaluated to identify high-confidence interactors. We detail the entire workflow of this approach.
CITATION STYLE
Wendrich, J. R., Boeren, S., Möller, B. K., Weijers, D., & De Rybe L, B. (2017). In vivo identification of plant protein complexes using IP-MS/MS. In Methods in Molecular Biology (Vol. 1497, pp. 147–158). Humana Press Inc. https://doi.org/10.1007/978-1-4939-6469-7_14
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