research groups
Protein Structure, Folding and Function
summary
Sede:
Email:
- Catalano Dupuy, Daniela L.
- Rosano, Germán Leandro
- Aguilar Lucero, Dianela
- Berrocal, Rodrigo
- Bertero, Fabricio
- Bianchimano Macat, Luciana
- Don, Carla
- Garavaglia, Macarena
- Cantoia, Alejo
RESEARCH LINES
Study of the structure-function relationship in molecular chaperones
The cellular proteome results from the balance of protein synthesis and degradation. The cell’s fate depends on its ability to maintain protein homeostasis (proteostasis). Disruption of the appropriate proteome for a given situation can significantly damage the cell and even its death.
Many mechanisms respond to proteome variations by regulated systems. These mechanisms are known as “protein quality control,” consisting of a network of molecular chaperones, proteases, and accessory proteins that eliminate damaged proteins, solubilize potentially toxic aggregates or assist in protein folding.
In certain situations, the protein quality control can get overloaded. For this reason, the cytosol and organelles trigger genetic programs resulting in the overexpression of gene coding for the protein quality control members. This process is known as unfolded protein response (UPR).
We study the conditions that set the UPR in motion and the communication of the stress to the nucleus. We are also interested in knowing the defense mechanisms that are activated in the cell to ensure its survival. We use techniques such as proteomics, western blots, plant transformation, and nuclear magnetic resonance. Directors: Dr. Germán Rosano / Dr. Eduardo Ceccarelli.
Study of the structure-function relationship in flavoenzymes
Ferredoxin-NADP+ reductases (FNR) constitute a family of monomeric proteins that contain non-covalently bound FAD as a prosthetic group. These widely distributed flavoenzymes are involved in the electron transfer of biologically important processes. FNRs catalyze the reversible electron transfer between NADP(H) and one-electron carriers such as ferredoxin or flavodoxin. They are classified as plant and mitochondrial-type. Plant-type FNRs are grouped into plastidic and bacterial classes. Bacterial FNRs participate in metabolic pathways, especially appropriate for developing antimicrobial agents because they are not present in humans. Thus, they can be used to design inhibitors in the fight against diseases caused by different pathogens.
Our studies aim to understand the catalytic mechanism of FNRs from plants and bacteria, and those relevant metabolic processes in which they participate, with particular emphasis on the structural characteristics that define their catalytic efficiency. We focus on the structural and functional analysis of FNRs and the identification and characterization of their natural substrates.
Our experimental approach includes analysis of recombinant wild-type and protein-engineered enzymes. We study enzymes by kinetic analysis, biophysical and structural methods, and modeling of protein structures and their substrates. Directors: Dr. Daniela Catalano Dupuy / Dr. Eduardo Ceccarelli.
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