Activity and regulation of cyanobacterial dynamin-like proteins

• Applicant: Professor Dr. Dirk Schneider
• Subject Area: Biochemistry ; Metabolism, Biochemistry and Genetics of Microorganisms ; Structural Biology
• Term: since 2025
• Project identifier: Deutsche Forschungsgemeinschaft (DFG) - Project number 562612330

The evolution of the multitude of internal membrane systems in eukaryotes was accompanied by the development of mechanisms for membrane remodeling, such as vesicular transport processes and mechanisms for the repair of damaged membranes. In prokaryotic cells, too, membrane processes have been established that were long considered eukaryotic-specific, such as the formation of intra- or extracellular vesicles, the formation of intracellular membrane systems, such as the thylakoid membranes in cyanobacteria, as well as membrane fusion and fission processes. Many proteins involved in membrane dynamics in eukaryotes have long been considered “eukaryotic inventions”. In recent years, however, an increasing number of such “typically eukaryotic” proteins that are crucial for membrane dynamics have also been identified in prokaryotes, including dynamin-like proteins (DLPs). DLPs are large mechanochemical enzymes that utilize the energy generated by GTP hydrolysis to remodel membranes by either membrane fusion or fission. Recently, we have obtained detailed information on the structure and activity of SynDLP, a novel DLP encoded in the cyanobacterium Synechocystis. Our observations are summarized in two recent reports published in Nature Communications (2023) and Cell Reports (2024). The proposed project aims to understand the physiological role of cyanobacterial DLPs that are likely to be involved in remodeling of internal membranes. We will use a combination of in vivo studies and biochemical and biophysical in vitro analyses, together with structural analyses (performed in collaboration), to reveal the structure and activity of novel bacterial DLPs. The following four questions will be addressed in the project: 1) How exactly does SynDLP bind to and remodel membranes? 2) How do structural changes induced by nucleotide binding regulate protein-protein contacts (and thus the activity of SynDLP)? 3) What is the in vivo function of SynDLP? 4) Does Synechocystis encode other DLPs and what are their specific structures and functions? The proposed analyses will significantly expand our understanding of the structure, activity and regulation of bacterial DLPs and DLPs in general and will allow us to better understand the biogenesis and dynamics of an intracellular membrane system.

• DFG Programme: Research Grants