Fascinating Insights into the Cell’s Repair System
The membrane that surrounds cells in living organisms is highly flexible and sensitive. How it protects itself from damage and renews is crucial for many life processes—and not yet fully understood in detail. However, scientists from Forschungszentrum Jülich from Helmholtz Information, Heinrich Heine University Düsseldorf, and Johannes Gutenberg University Mainz have now gained fascinating new insights using cryo-electron microscopy. For example, the membrane protein Vipp1, which occurs in the photosynthesis apparatus of plants, algae, and bacteria, can form various structures that could serve as tools to stabilize and reinforce the cell membrane when needed. (Source: Forschungszentrum Jülich – Press Releases)
In a second study, the researchers also gained new insights into the function of the related protein PspA, found in bacteria. Both molecules, Vipp1 and PspA, are unusually plastic and can adopt various structures, forming rings and tubes with different diameters.
Scientific Results
The cell membrane has numerous essential functions: it protects the cell interior from the environment, allows nutrients to enter, expels waste products, and transmits signals between cells. Despite its central role, the cell membrane is also very sensitive. It consists of a thin layer of lipids that, while protective, is also susceptible to stress from physical pressure and stretching or chemical influences. Environmental factors like UV radiation or toxins can also damage the membrane.
In plant cells, for example, intense light can severely stress and even damage the membranes in chloroplasts, where photosynthesis occurs. Proteins like Vipp1 are therefore essential for cell survival, as they protect membrane structures and repair them when needed.
The precise mechanism is not yet fully understood. Thanks to state-of-the-art cryo-electron microscopes at the Jülich-based Ernst Ruska-Centre, the researchers have now gained new insights into the interaction between Vipp1 and the cell membrane. They discovered that Vipp1 forms carpet-like structures on the cell membrane, stabilizing it. They also found ring complexes and tubes made of Vipp1 filled with membrane, which could potentially “pinch off” damaged membrane areas or even connect two separate membranes.
Societal and Scientific Relevance
The studies provide new insights into the ability of the proteins Vipp1 and PspA to alter cell membranes and protect vital processes within cells. These discoveries could, in the future, contribute to the development of new biotechnological applications, such as the production of biomaterials or the optimization of photosynthesis in plants. Vipp1 is particularly important as it is involved in the formation and maintenance of thylakoid membranes—membranes in the chloroplasts of plant cells where the light reactions of photosynthesis take place, converting light into chemical energy.
Interestingly, the underlying mechanism shows a strong resemblance to ESCRT-III proteins, which are highly conserved in human cells—meaning they have remained largely unchanged throughout evolution, indicating an essential function. Therefore, a better understanding of the structure and function of these proteins could lead to the development of new drugs, such as antibiotics targeting processes in cellular membranes.
Further Details
In both studies, state-of-the-art cryo-electron microscopes from the Ernst Ruska-Centre (ER-C) at Forschungszentrum Jülich were used. These enabled researchers to study the proteins at atomic resolution and in an unusually high number of structural states, as well as to observe the interactions between the proteins and the membranes. The work is part of an established collaboration with the research group of Prof. Dirk Schneider, Johannes Gutenberg University Mainz, which has been ongoing for years.
FZJ/T. Schlößer, 08.10.2024
Note: The article has been translated from German to English. It is based on a press release from FZJ.
The original press release can be found at:
Faszinierende Einblicke ins Reparatursystem der Zelle (only in german)
The original publication can be found at (Open Access):
Structural basis for Vipp1 membrane binding: From loose coats and carpets to ring and rod assemblies;
Benedikt Junglas, David Kartte, Mirka Kutzner, Nadja Hellmann, Ilona Ritter, Dirk Schneider, Carsten Sachse; Nat Struct Mol Biol (2024), DOI: 10.1038/s41594-024-01399-z
Benedikt Junglas, Esther Hudina, Philipp Schönnenbeck, Ilona Ritter, Anja Heddier, Beatrix Santiago-Schübel, Pitter F. Huesgen, Dirk Schneider & Carsten Sachse: Structural plasticity of bacterial ESCRT-III protein PspA in higher-order assemblies; Nat Struct Mol Biol (2024), DOI: 10.1038/s41594-024-01359-7
Location in Helmholtz Information:
Helmholtz Information, Program 3: Materials Systems Engineering Processing, Topic 5: Materials Information Discovery
Contact:
Prof. Dr. Carsten Sachse
Ernst Ruska-Centre for Microscopy and Spectroscopy with Electrons (ER-C)
Ernst-Ruska-Centrums for Structural Biology (ER-C-3)
Forschungszentrum Jülich
Phone: +49 2461/61-2030
E-Mail: c.sachse@fz-juelich.de
Prof. Dr. Benedikt Junglas
Ernst Ruska-Centre for Microscopy and Spectroscopy with Electrons (ER-C)
Ernst-Ruska-Centrums for Structural Biology (ER-C-3)
Forschungszentrum Jülich
Phone: +49 2461/61-3130
E-Mail: b.junglas@fz-juelich.de
Contact for this press release:
Tobias Schlößer
Press Officer
Forschungszentrum Jülich
Phone: +49 2461 61-4771
E-Mail: t.schloesser@fz-juelich.de
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Readers comments (1)
Hela Cells
This blog offers a captivating exploration of the cell’s repair system, particularly focusing on the proteins Vipp1 and PspA and their roles in membrane stabilization. The research provides groundbreaking insights into cellular repair mechanisms through the use of advanced cryo-electron microscopy. The potential applications of these findings, from improving photosynthesis to developing antibiotics, highlight the far-reaching impact of this work. Truly a fascinating read for anyone interested in the intersection of molecular biology and biotechnology.