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Department of Pharmacy and Biotechnology - FABIT

Molecular Plant Physiology. Coordinator: Trost

Photosynthetic organisms remove carbon dioxide from the atmosphere, providing our planet with food, feed and energy (biofuels). The laboratory is engaged in studying the molecular basis of primary carbon metabolism in both terrestrial and aquatic photosynthetic model organisms.

Areas: Industrial, plant and environmental biotechnologies
Glyceraldehyde-3-phosphate dehydrogenase (background) is an example of a metabolic enzyme that is post-translationally regulated through various types of cysteines redox modifications. We study this type of metabolic regulation in model photosynthetic organisms such as Arabidopsis (bottom left), Chlamydomonas (center), and Physcomitrium (right).

Research themes

Carbon metabolism

The project is focused on the study of the different pathways of carbon metabolism (Calvin-Benson cycle, primary starch degradation, glycolysis and alcoholic fermentation). The aim of our research is to shed light on the enzymatic regulation mediated by redox post-translational modifications. Along with that, we study how the formation of supramolecular complexes and protein aggregation influence cellular proteostasis. Our research activity includes both physiological analyses on the model plant Arabidopsis thaliana and biochemical and structural studies on recombinant proteins.

Redox homeostasis

Ascorbate and glutathione are the main regulators of redox homeostasis in plant cells. Moreover, glutathione is involved in important redox modifications of the proteome such as S-glutathionylation and S-nitrosylation. Our research project involves the use of model organisms (both wild type and transgenic), including the unicellular algae Chlamydomonas reinhardtii, the bryophyte Physcomitrium patens e the higher plant Arabidopsis thaliana. Our aim is to study the functionality of several enzymatic systems, both soluble and trans-membrane, which are involved in cellular redox homeostasis during development and in various stress conditions. These in vivo studies are supported by in vitro analysis of proteins that are essential for the redox homeostasis of protein thiols (thioredoxins and glutaredoxins), glutathione (glutathione reductase, S-nitrosoglutathione reductase) and ascorbate (cytochromes b-561).

Lab members

Paolo Trost, Full Professor 

Francesca Sparla, Associate Professor 

Mirko Zaffagnini, Associate Professor 

Libero Guerrieri, Junior Assistant Professor  

Maria Meloni, Research Fellow

Sayyeda Hira Hassan, Research Fellow

Tancredi Bin,  Research Fellow

Ginevra Marie Eloise Peppi, PhD Student

Anna Clara Capuzzi, PhD Student

Internship projects

Each Academic Year the Molecular Plant Physiology laboratory provides 9 internships for bachelor’s degree students and 3 internships for master’s degree students. Preferably, we provide positions for students of Biological Sciences (bachelor's degree), Biotechnology (bachelor's degree), Genomics (bachelor’s degree), Biology of Human and Environmental Health (bachelor's degree), Molecular and Cell Biology (master's degree), Sciences and Management of Nature (masters’s degree) and Plant and Agriculture Biotechnology (masters’s degree).

Main publications

  • Gradogna, A., Lagostena, L., Beltrami, S., Tosato, E., Picco, C., Scholz-Starke, J., Sparla, F., Trost, P., Carpaneto, A. (2023) “Tonoplast cytochrome b561 is a transmembrane ascorbate-dependent monodehydroascorbate reductase: functional characterization of electron currents in plant vacuoles.” New Phytol. 238:1957-1971. https://doi.org/10.1111/nph.18823
  • Gurrieri, L., Fermani, S., Zaffagnini, M., Sparla, F., Trost P. (2021) Calvin-Benson cycle regulation is getting complex. Trends Plant Sci. 26(9):898-912. https://doi.org/10.1016/j.tplants.2021.03.008
  • Tagliani, A., Rossi, J., Marchand, C. H., De Mia, M., Tedesco, D., Gurrieri, L., Meloni, M., Falini, G., Trost, P., Lemaire, S. D., Fermani, S., & Zaffagnini, M. (2021). Structural and functional insights into nitrosoglutathione reductase from Chlamydomonas reinhardtii. Redox biology, 38, 101806. https://doi.org/10.1016/j.redox.2020.101806
  • Zaffagnini, M., Marchand, CH., Malferrari, M., Murail, S., Bonacchi, S., Genovese, D., Montalti, M., Venturoli, G., Falini, G., Baaden, M., Lemaire, S.D., Fermani, S., Trost, P. (2019) “Glutathionylation primes soluble glyceraldehyde-3-phosphate dehydrogenase for late collapse into insoluble aggregates”. Proc Natl Acad Sci U S A. 116 (51):26057–26065. https://www.pnas.org/content/116/51/26057.long
  • Gurrieri, L., Del Giudice, A., Demitri, N., Falini, G., Pavel, N.V., Zaffagnini, M., Polentarutti, M., Crozet, P., Marchand, C.H., Henri, J., Trost, P., Lemaire, S.D., Sparla, F., Fermani, S. (2019) “Arabidopsis and Chlamydomonas phosphoribulokinase crystal structures complete the redox structural proteome of the Calvin-Benson cycle”. Proc Natl Acad Sci U S A. 16;116(16) 8048-8053. https://www.pnas.org/content/116/16/8048.long

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