Chapter title |
Mapping Protein–Protein Interactions Using Affinity Purification and Mass Spectrometry
|
---|---|
Chapter number | 15 |
Book title |
Plant Genomics
|
Published in |
Methods in molecular biology, April 2017
|
DOI | 10.1007/978-1-4939-7003-2_15 |
Pubmed ID | |
Book ISBNs |
978-1-4939-7001-8, 978-1-4939-7003-2
|
Authors |
Chin-Mei Lee, Christopher Adamchek, Ann Feke, Dmitri A. Nusinow, Joshua M. Gendron |
Editors |
Wolfgang Busch |
Abstract |
The mapping of protein-protein interaction (PPI) networks and their dynamics are crucial steps to deciphering the function of a protein and its role in cellular pathways, making it critical to have comprehensive knowledge of a protein's interactome. Advances in affinity purification and mass spectrometry technology (AP-MS) have provided a powerful and unbiased method to capture higher-order protein complexes and decipher dynamic PPIs. However, the unbiased calling of nonspecific interactions and the ability to detect transient interactions remains challenging when using AP-MS, thereby hampering the detection of biologically meaningful complexes. Additionally, there are plant-specific challenges with AP-MS, such as a lack of protein-specific antibodies, which must be overcome to successfully identify PPIs. Here we discuss and describe a protocol designed to bypass the traditional challenges of AP-MS and provide a roadmap to identify bona fide PPIs in plants. |
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