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Basis for the essential cellular powerhouses

Date:
January 15, 2021
Source:
University of Freiburg
Summary:
Researchers have solved the operating mode of the barrel pore protein assembly in the mitochondrial outer membrane.
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Researchers have solved the operating mode of the barrel pore protein assembly in the mitochondrial outer membrane.

Mitochondria are vital for the human body as cellular powerhouses: They possess more than 1,000 different proteins, required for many central metabolic pathways. Disfunction of these lead to severe diseases, especially of the nervous system and the heart. In order to transport proteins and metabolites, mitochondria contain a special group of so-called beta-barrel membrane proteins, which form transport pores in the outer mitochondrial membrane. So far, scientists have not been able to explain the operating mode of the sorting and assembly machinery (SAM) for the biogenesis of these beta-barrel proteins. A team led by Prof. Dr. Toshiya Endo from Kyoto University/Japan, Prof. Dr. Nils Wiedemann and Prof. Dr. Nikolaus Pfanner from the University of Freiburg and Prof. Dr. Thomas Becker from the University of Bonn has now solved the structure and function of the SAM complex. The researchers have published their results in the journal Nature.

The SAM complex consists typically of two beta-barrel subunits named Sam50, which are capped on their outside by the two additional subunits Sam35 and Sam37. The researchers found that while the SAM complex forms a new beta-barrel protein, it contains only one Sam50. The second beta-barrel subunit functions as a flexible placeholder: it temporarily leaves the SAM complex, freeing the space for the new beta-barrel protein to form. This dynamic mechanism suggests how a new beta-barrel protein can mature to full size in the SAM complex and only be released as a completely folded protein. "This enabled us to identify a new principle for the formation of membrane proteins that perform vital functions in our cells," explains Wiedemann.


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Materials provided by University of Freiburg. Note: Content may be edited for style and length.


Journal Reference:

  1. Hironori Takeda, Akihisa Tsutsumi, Tomohiro Nishizawa, Caroline Lindau, Jon V. Busto, Lena-Sophie Wenz, Lars Ellenrieder, Kenichiro Imai, Sebastian P. Straub, Waltraut Mossmann, Jian Qiu, Yu Yamamori, Kentaro Tomii, Junko Suzuki, Takeshi Murata, Satoshi Ogasawara, Osamu Nureki, Thomas Becker, Nikolaus Pfanner, Nils Wiedemann, Masahide Kikkawa, Toshiya Endo. Mitochondrial sorting and assembly machinery operates by β-barrel switching. Nature, 2021; DOI: 10.1038/s41586-020-03113-7

Cite This Page:

University of Freiburg. "Basis for the essential cellular powerhouses." ScienceDaily. ScienceDaily, 15 January 2021. <www.sciencedaily.com/releases/2021/01/210115110316.htm>.
University of Freiburg. (2021, January 15). Basis for the essential cellular powerhouses. ScienceDaily. Retrieved May 24, 2024 from www.sciencedaily.com/releases/2021/01/210115110316.htm
University of Freiburg. "Basis for the essential cellular powerhouses." ScienceDaily. www.sciencedaily.com/releases/2021/01/210115110316.htm (accessed May 24, 2024).

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