Program no. DSMBBC/2024/3 Study of the mechanism of sulfur remobilization and translocation in Arabidopsis thaliana plants
Offer DescriptionBackground: Sulfur (S) deficiency became an agricultural problem several decades ago due to reduced S deposition by industrial facilities. Plants from the Brassicaceae family (including rapeseed, cabbage, and the model plant Arabidopsis thaliana) produce S-rich secondary metabolites, and limiting S supply can significantly affect the quantity and quality of their yield. When nutrients are scarce, plants adapt by using them more efficiently. During vegetative development leaves represent a major store of nutrients that can be remobilized thereafter to sustain the growth of reproductive tissues. Autophagy, a conserved eukaryotic degradation pathway, removes unnecessary cytoplasmic components and damaged organelles in leaves and facilitates the release of nutrients and their storage in developing seeds. The autophagy mutants accumulate a large amount of proteins in leaves during senescence, however, they translocate less than 50% of S to the seeds. Several proteins connected directly with S metabolism have been implicated to play a role in efficient S assimilation and remobilization. The sulfur dioxygenase ETHE1 catalyzes the oxidation of persulfides to sulfite and has a key function in situations of high protein turnover, such as seed production. ETHE1 is also an indirect positive regulator of autophagy, as it consumes sulfide that negatively impacts autophagy. LSU genes are strongly induced by S deficiency and encode small proteins involved in multiple protein interactions. The partners of LSU proteins are functionally diverse, suggesting that LSU have a complex regulatory role in various processes. Studies in our lab have shown that LSU proteins may impact S assimilation rate. Additionally, they may also play a role in autophagy by interacting with autophagy receptor.Activity proposed: The project aims to elucidate the mechanism of S remobilization and translocation, which may increase plant S use efficiency. The work will concentrate on the molecular characterization of three Arabidopsis mutants: atg5, ethe1, q-lsu. These mutants have a similar metabolic profile regarding S compounds: increased sulfate, cysteine and glutathione concentrations in leaves (q-lsu has fewer of these compounds in roots) and lower S content in seeds, suggesting defects in S remobilization. By feeding the plants with isotopes of nitrogen (15N) and sulfur (34S) their partitioning to different tissues will be established. The careful examination of the proteomes of leaves and seeds will help to establish which processes are affected in the mutants. Based on this result the transcription level of selected genes will be monitored. The long-term goal will be the identification of proteins involved in S remobilization, especially those with undefined functions, and tracing their role. This will be achieved by the construction of knock-out mutants (CRISP/Cas9 technology) or overexpressants and assaying plant performance in different S regimes. To monitor the spacio-temporal protein location the YFP fusion proteins will be observed by confocal fluorescent microscopy. This work will provide not only new insights into S remobilization processes but also the potential targets for further dissection of molecular mechanisms adapted by plants during S deficiency stress. The project will be realized in collaboration with Prof. Céline Masclaux-Daubresse, Institut Jean-Pierre Bourgin, Versailles, France.RequirementsResearch Field Biological sciences Education Level Master Degree or equivalentSkills/Qualifications
Languages ENGLISH Level GoodResearch Field Biological sciencesAdditional InformationBenefits
Surcharge for the multi sport card, parking, optional language coursesSelection processThe recruitment process consists of two stages: * selection of candidates by the Committee based on their previous achievements and academic performance presented in the documents submitted; for each position no more than 5 applicants who have achieved the highest scores, but no less than 60% of the maximum points, shall be qualified for the next stage;
Stage One
Stage Two
Website for additional job detailsWork Location(s)Number of offers available 1 Company/Institute Institute of Biochemistry and Biophysics Polish Academy of Sciences Country Poland City Warsaw Postal Code 02-106 Street ul. Pawińskiego 5aWhere to apply WebsiteContact CityWarsaw WebsiteStreetul. Pawińskiego 5a Postal Code02-106 E-MailPhDschool-recruitment@ibb.waw.plSTATUS: EXPIRED
Warszawa, mazowieckie
Thu, 02 May 2024 04:04:23 GMT
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