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Researchers from the Ruhr-Universität Bochum and the University of Tübingen have gained new knowledge on the structure of the Bax killer protein.
Protein induces programmed cell death, a method by which the body has cells that are no longer needed or have been pathologically altered. As Bax constantly changes location in the cell, its structure is difficult to study.
The team led by Enrica Bordignon and Stephanie Bleicken, both from the Bochum-based EPR spectroscopy working group, describes new information about Bax in the journal Cell death and differentiation.
The work was carried out within the framework of the Cluster of Excellence Ruhr Explores Solvation (Resolv).
Cell death is essential to life
Every second, about a million cells die in the body as a result of programmed cell death, also called apoptosis. Disruptions in this mechanism can be life threatening as they can trigger cancer or neurodegenerative diseases. A group of proteins, Bcl-2 proteins, including Bax, play a crucial role in apoptosis.
"These proteins are difficult to study because they pass from the aqueous cell fluid to the mitochondrial membrane," Bleicken said. "The active form of membrane-integrated protein, in particular, can only be studied with a small number of methods."
Most likely structural model identified
The team used different spectroscopic methods to study Bax. They recorded both the structure of the Bax form incorporated in the membrane and its interactions with the solvent, namely water or lipids. The researchers then compared these data with previously published information on the topology of the protein and examined the results compatible with each other.
"We evaluated all existing structural models and identified the most likely topology model for the active structure of Bax in the membrane," Bordignon said.
To induce apoptosis, Bax creates a hole in the membrane of the mitochondria, which represents the power plants of the cells.
Bochum researchers also hope to use other methods to study the protein directly on the membrane of isolated mitochondria. In addition, they wish to further analyze the interaction of Bax with the surrounding water molecules at temperatures such as those found in the body. The Bordignon group has developed the necessary methods as part of Resolv.
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