Abstract
Phytohormones tightly regulate plant growth by integrating changing environmental and developmental cues. Although the key players have been identified in many plant hormonal pathways, the molecular mechanisms and mode of action of perception and signaling remain incompletely resolved. Characterization of protein partners of known signaling components provides insight into the formed protein complexes, but, unless quantification is involved, does not deliver much, if any, information about the dynamics of the induced or disrupted protein complexes. Therefore, in proteomics research, the discovery of what actually triggers, regulates or interrupts the composition of protein complexes is gaining importance. Here, tandem affinity purification coupled to mass spectrometry (TAP-MS) is combined with label-free quantification (LFQ) to a highly valuable tool to detect physiologically relevant, dynamic protein–protein interactions in Arabidopsis thaliana cell cultures. To demonstrate its potential, we focus on the signaling pathway of one of the most recently discovered phytohormones, strigolactones.
Highlights
Plants produce a broad range of phytohormones, which are small molecules that regulate their growth and development and control their responses to biotic and abiotic stresses, locally as well as throughout the entire plant
The SMXL7 sensitivity to rac-GR24 was tested in cell cultures expressing 35S::GSrhino- SMXL7 as for 35S::GSrhino-SMXL7 and the SMXL7 protein level did not decrease upon treatment with rac-GR24, in agreement with previously published data (Jiang et al, 2013; Soundappan et al, 2015) (Figure 1C)
The quantitative TAP (qTAP) might data shed new light on the dynamics of protein complexes formed around SMXL7 in response to strigolactones
Summary
Plants produce a broad range of phytohormones, which are small molecules that regulate their growth and development and control their responses to biotic and abiotic stresses, locally as well as throughout the entire plant. Proteins that are crucial for the perception and the transduction of molecular signals, such as phytohormones, often form complexes to fulfill their biological function. Most of the protein– protein interactions (PPIs) are not static, but rather dynamic, because they are constantly subjected qTAP and Changes in Protein Complex Composition to changes in the crowded cellular environment. Knowledge of the interaction partners of a given protein may provide insight into its function at the molecular level or into the process in which it is involved. Quite some methods exist to detect PPIs, for a better understanding of cellular mechanisms, the identification of functionally relevant PPIs and, in particular, the characterization of how they are influenced by varying physiological conditions are required (Buntru et al, 2016)
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