Final Report Summary - STRESS-PROTEOSTASIS (System-wide analysis of intrinsic protein properties affecting proteome homeostasis upon abiotic stress in green algae)
The project entitled “System-wide analysis of intrinsic protein properties affecting proteome homeostasis upon abiotic stress in green algae” sits at the nexus between systems biology and protein biochemistry to elucidate components causing proteotoxicity during the onset of heat stress. Stress-induced deleterious changes within the proteome mostly result from an increased rate of protein misfolding and aggregation, which in turn can result in cellular dysfunction or lethality.
With global warming, crop plants more frequently experience severe environmental changes. Hence, it is important to acquire a deeper understanding of plant protein homeostasis in order to succeed with the engineering of more stress tolerant crop plants. The presented study aims to investigate protein homeostasis changes on a system level and to characterize the proteins sensitive to stress-mediated conformational damage. Here, the green alga Chlamydomonas reinhardtii served as a model system to study how heat-exposure affects protein aggregation, refolding and degradation in photosynthetically active organism. This project was set up, to identify and characterize proteins which are either unfolded or degraded during stress or which are sequestered in insoluble aggregates. These aims were pursued by comprehensive quantitative-proteomics approaches and the bioinformatic analyses of stress-affected proteins under various conditions.
With global warming, crop plants more frequently experience severe environmental changes. Hence, it is important to acquire a deeper understanding of plant protein homeostasis in order to succeed with the engineering of more stress tolerant crop plants. The presented study aims to investigate protein homeostasis changes on a system level and to characterize the proteins sensitive to stress-mediated conformational damage. Here, the green alga Chlamydomonas reinhardtii served as a model system to study how heat-exposure affects protein aggregation, refolding and degradation in photosynthetically active organism. This project was set up, to identify and characterize proteins which are either unfolded or degraded during stress or which are sequestered in insoluble aggregates. These aims were pursued by comprehensive quantitative-proteomics approaches and the bioinformatic analyses of stress-affected proteins under various conditions.