Cells are composed of many proteins, that assemble into various protein complexes.
In a densely crowded cell, how do these proteins find each other in a cell?
How do these activities affect plant growth and plant immunity?
At the Ahn Lab, we study how plant protein complexes are assembled, and how this assembly affects plant immunity.
Plant immune receptors are crucial for the plants to detect pathogens and protect itself from infection.
Intracellular immune receptors are of particular interest, as many of these receptors are used for disease resistance breeding.
However, these proteins are expressed low in abundance, in order to prevent over-accumulation that lead to unregulated immune activation that can lead to growth arrest and cell death.
Yet, a crucial step in activation of these intracellular immune receptors is ‘oligomerization.’
We investigate how plant intracellular immune receptors are kept low in abundance, but can also be rapidly oligomerized.
(Below image: Experimental procedure of blue native-PAGE experiment. Proteins are extracted from leaves, and loaded onto blue-native PAGE. Larger protein complexes are separated from smaller protein complexes. Right-most panel shows actual blue native-PAGE image of RubisCO complex, one of the most abundant protein complexes on Earth. Image adapted and modified from Ahn, Lin et al. (2023) EMBO J.)
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Many plant species have undergo gene duplication events throughout their evolution.
While gene duplication can be a dangerous event, some genes have gained new function for survival.
But how does gene duplication affect the function of protein complexes made of many different genes?
Using model protein complexes, we want to understand how gene duplication affects protein complex assembly in plants.
(Below image: Schematic drawing of how gene duplication generates different protein complexes. Duplication of gene A in to A-1 and A-2 leads to formation of different protein complexes.)
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