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Our research focuses on investigation of  plant mitochondrial and plastidial proteostasis. We employ a protein turnover analysis platform that couples metabolic labelling and mass spectrometry to investigate degradation and synthesis rates of specific proteins (Li et al, Plant Cell, 2017). This is a new strategy to understand the photodamage to chloroplast,

chaperone and protease functionality, and autophagic flux in modulation of mitochondrial and chloroplast proteostasis.

1. Investigation of Lon1 associated proteins and autophagy degradation in mitochondrial protein homeostasis and turnover. 

In organelles, protein turnover is modulated externally through mitochondria‐targeted gene expression and internally by proteolysis and chaperones that act post‐translationally on the organelle proteome.  Plant mitochondria, plastids and peroxisome are predicted to contain ~200 peptidases, proteases and chaperones for internal protein quality control (van Wijk, 2015) but only a small number of these proteins have characterized functions. This project aims to explore Lon1 associated proteins and autophagy activity in maitenaince of mitochondrial proteostasis and turnover. 
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2. Investigation of unstable photosynthetic protein targets under light stress.

This project aims to answer unresolved questions regarding novel rapidly degrading plastidial photosynthesis complex proteins. We will assess how light and phosphorylation affect the degradation process and determine how these proteins are synthesised to maintain homeostasis. This project will use protein turnover and protease degradation determination techniques to analyse unstable protein targets under varying light conditions. The result will be better understanding of how these fast degrading proteins are linked with photoinhibition and provide insight into previously unresolved questions. This research will increase crop yield by providing a foundation for future development of photoinhibition tolerant and more robust crops.
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