ChloroQuality · Dissecting chloroplast protein quality control specificity for rational plant reprogramming
Horizon 2020 — Marie Skłodowska-Curie Actions
- Duration
- 2016-01-01 → 2017-12-31
- EU contribution
- €159,461
- Participants
- 1
- Scheme
- MSCA-IF-EF-ST
Lines connect the coordinator with its partners.
Results in brief
Dissecting chloroplast protein quality control specificity for rational plant reprogramming
Chloroplasts are specialized compartments (organelles) of the cell that are essential in plants and algae for photosynthesis. In the thylakoid membrane of the chloroplast, photosynthetic complexes harvest the light energy allowing the fixation of carbon dioxide and the subsequent production of nutrients for plants. Furthermore, the biosynthesis of important compounds including pigments and plant hormones is performed in this organelle. Therefore, chloroplasts play a primary role in plant development and fitness. While the composition and structure of chloroplastic high molecular protein complexes such as photosystems or ribosomes is well characterized, less information is available about their regulation, specially under stress situations. Similarly to other compartments, chaperones and proteases are required to monitor protein homeostasis in the chloroplast, assisting the folding, assembly and degradation of proteins during their lifetime. Although several types of chaperones are known to assist in the correct functioning of the chloroplast, the molecular basis behind these requirements remain unknown. Thus, it is necessary to increase our understanding of how the levels and the activity of chloroplastic proteins are regulated. ChloroQuality address this challenge by studying the DNAJ protein family of chaperones in the plant model Arabidopsis thaliana.
Data: CORDIS, © European Union
Project objective
Improving food quality, crop productivity and plant resistance to stresses are major demands of Europe’s society and economy. Plants are sessile organisms that have developed very flexible strategies to cope with adverse environmental conditions as heat, cold, drought and salt stress. These stresses cause protein misfolding and aggregation resulting in plant damage/death and productivity losses. Recycling of damaged proteins is achieved by the action of molecular chaperones. But when recycling is not possible, toxic aggregated proteins have to be degraded by the action of proteases to avoid cellular damage. Chaperones and proteases act coordinately and constitute the protein quality control system that is essential for plant survival. In plant chloroplasts, the chaperone Hsp70 is known to posttranslationally regulate important processes like photosynthesis. It is known that the specificity of Hsp70 is determined by its J-protein partners, adaptors that recognize unfolded substrates and transfer them to the chaperone for refolding. However, little is known about the target proteins of Hsp70, such that there is a large lack of information about how chloroplastic enzymes are regulated at protein levels. This knowledge is crucial for rational engineering of specific molecular pathways and plant fitness improvement. The ability to specifically alter plant metabolism without undesirable effects is a fundamental demand of European society and addresses current concerns about transgenic plants. This proposal aims to cover this gap by discovering and validating interactors of chloroplastic J-proteins. The strong background of the applicant in protein quality control and the expertise in chloroplast biology of the receiving group will synergistically contribute to shed light on the chloroplast signaling network. In addition, this project aims to develop the candidate into an independent scientist and open his own line of investigation.
Original text from CORDIS.
Participants
- LUDWIG-MAXIMILIANS-UNIVERSITAET MUENCHEN · PlaneggCoordinatorGermany
Links
- View on CORDIS
- DOI: 10.3030/656822
- http://plantmolecularbiology.bio.lmu.de/research/plant-acclimation/chloroplast-protein/index.html
Data: CORDIS, © European Union