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The dynamic structure of protein domains within the cytoplasmic membrane of Escherichia coli

Project description

Bacterial protein dynamics in the cell membrane

In bacteria, membrane proteins are crucial for maintaining cellular functions, including nutrient transport, waste removal, and energy generation through processes like photosynthesis. They also play a key role in processes such as protein translocation, quality control, and peptidoglycan synthesis, but how they assemble and disassemble within membrane domains remains unclear. With the support of the Marie Skłodowska-Curie Actions programme, the MemProDx project is investigating the dynamic organisation of membrane protein domains in the inner membrane of Escherichia coli. Using cutting-edge imaging techniques, the research team will explore the movement and distribution of these protein domains under various conditions, including stress and antibiotic exposure. The study is expected to provide fundamental insight into chemotaxis and pathogen-host interactions.

Objective

Membrane proteins govern how bacteria inside the human body, animals, plants, water sources or soil interact with their environment. Membrane proteins show intricate spatial organization and can be compartmentalized in the membrane, but it is unknown how they dynamically assemble and vanish from membrane domains. In this project, I aim to reveal the dynamic organization of membrane protein domains in the inner membrane of Escherichia coli. I will examine the distribution and dynamics of proteins that engage in protein domains and play crucial roles in the distribution of other proteins in the membrane. These proteins are responsible for functions like membrane protein translocation, quality control, lipid raft formation, and synthesis of the peptidoglycan scaffold. By employing live-cell super-resolution and single-molecule fluorescence imaging, I will observe the assembly, movement, and variations in size and content of protein domains within growing bacterial cells. I will investigate the impact of external conditions like heat- and osmotic stress, starvation, and antibiotics on the dynamics of membrane protein domains. This proposal addresses a fundamental gap in our understanding of the organization of proteins in bacterial membranes and thus offers insights into various processes from chemotaxis to pathogen-host interactions. The development of super-resolution fluorescence microscopy protocols for imaging membrane proteins in live bacterial cells will be a methodological achievement, enabling further advancements in the field.

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Coordinator

RIJKSUNIVERSITEIT GRONINGEN
Net EU contribution
€ 187 624,32
Address
Broerstraat 5
9712CP Groningen
Netherlands

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Activity type
Higher or Secondary Education Establishments
Links
Total cost
No data