Stress-proteostasis · System-wide analysis of intrinsic protein properties affecting proteome homeostasis upon abiotic stress in green algae
FP7 — People (Marie Curie Actions)
- Duration
- 2014-03-01 → 2018-02-28
- EU contribution
- €100,000
- Participants
- 1
- Scheme
- MC-CIG
Lines connect the coordinator with its partners.
Results in brief
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.
Data: CORDIS, © European Union
Project objective
Abiotic environmental stresses such as extreme temperatures represent serious threats to plants and are a main reason for significant agricultural crop losses every year. Hence, an understanding of the molecular consequences of stress exposure and the underlying principles of plant stress responses are fundamental questions in biology and provide the basis for the genetic engineering of stress resistant crop plants. In particular, high temperature stress leads to an increase in protein unfolding, misfolding, and aggregation and thus challenges proteome homeostasis (proteostasis). As a response, cells increase the expression of molecular chaperones to maintain proteostasis by counteracting protein misfolding and aggregation.The overall goal of this study is to globally identify properties of fragile proteins in plant proteomes challenged by heat-shock exposure. We will use the unicellular green algae Chlamydomonas reinhardtii and Nannochloropsis sp. as model organisms to monitor protein misfolding and aggregation under physiological conditions, mild stress and severe temperature stress. We will apply quantitative proteomics and bioinformatics to reveal physicochemical properties characteristic for proteins prone to misfolding and aggregation. By this, we will further identify proteins that have a high dependence on protection by molecular chaperones. Based on this system-wide analysis individual proteins will be engineered with the goal to optimize their conformational stability for improved stress tolerance.
Original text from CORDIS.
Participants
- RHEINLAND-PFALZISCHE TECHNISCHE UNIVERSITAT · KaiserslauternCoordinatorGermany
Links
Data: CORDIS, © European Union