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TurboID-Based Proximity Labeling for In Planta Identification of Protein-Protein Interaction Networks
Published on: May 17, 2020
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Identification of Phytaspase Interactors via the Proximity-Dependent Biotin-Based Identification Approach
Anastasia D Teplova1, Marina V Serebryakova2, Raisa A Galiullina2
1Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow 119991, Russia.
International Journal of Molecular Sciences
|December 10, 2021
Summary
Phytaspase, a plant subtilase, interacts with endoplasmic reticulum proteins like calreticulin-3 during programmed cell death. This finding sheds light on subtilase regulatory roles in plant stress responses and senescence.
Area of Science:
- Plant molecular biology
- Enzymology
- Cellular signaling
Background:
- Proteolytic enzymes, particularly subtilases, play crucial roles in plant development and senescence.
- Phytaspase is a plant subtilase implicated in stress-induced programmed cell death.
Purpose of the Study:
- To identify protein partners of phytaspase, a plant subtilase.
- To investigate the regulatory functions of phytaspase in plant stress responses.
Main Methods:
- Proximity-dependent biotin identification using TurboID in *Nicotiana benthamiana*.
- In vitro binding assays with purified proteins.
Main Results:
- Several intracellular protein interactors of phytaspase were identified, primarily soluble endoplasmic reticulum residents like endoplasmin, BiP, and calreticulin-3.
- Direct interaction between phytaspase and calreticulin-3 was confirmed.
- Phytaspase overexpression altered calreticulin-3 post-translational modification.
Conclusions:
- Phytaspase interacts with endoplasmic reticulum proteins, suggesting a role in regulating protein homeostasis and cellular processes.
- Calreticulin-3 is a direct interaction partner of phytaspase, with implications for programmed cell death and senescence pathways.
