Allegra Wundersitz (RWTH Aachen University)
Allegra Wundersitz's Master thesis was awarded with the Prize for the Best Plant Science Master Thesis, which was carried out at RWTH Aachen University in the year 2024 with the title:
Exploring the role of long-chain acyl-CoA esters in ACBP1-RAP2.12 complex stability
Wundersitz investigated how long-chain acyl-coenzyme A (CoA) esters facilitate the dissociation of the transcription factor RAP2.12 from ACBP1, providing new insights into oxygen sensing and acyl-CoA signaling in plants.
Long-chain acyl-coenzyme A (CoA) esters are key signaling molecules that initiate the hypoxic stress response in plants by promoting the dissociation of the transcription factor RAP2.12 from ACBP1 at the plasma membrane. This thesis investigates the molecular mechanism underlying the acyl-CoA-mediated protein dissociation using in silico, in vivo, and in vitro approaches. Protein-protein interaction assays suggest that RAP2.12 binds to the acyl-CoA-binding domain of ACBP1. Molecular dynamics simulations suggest that unsaturated acyl-CoAs may block the RAP2.12 binding site, thereby facilitating its release. Additionally, an ACBP1 mutant with reduced acyl-CoA affinity was generated by targeted site directed mutagenesis, to further explore the role of the ACBP1-acyl-CoA interaction in signal transduction. Preliminary measurements indicate a reduced binding affinity, making this mutant a useful tool for upcoming experiments. Overall, this work provides foundational insights into acyl-CoA-mediated signal transduction and could eventually contribute to the development of new strategies to enhance stress resistance in plants.
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Allegra Wundersitz conducted this work at the Institute of Biology I, Molecular Ecology of the Rhizosphere, in the working group of Prof. Dr. Joost T. van Dongen.
