Nature: Reveals the mechanism of action of mitochondrial seism selection and assembly complex

In a new study, Professor Toshiya Endo of Kyoto University in Japan, Professor nils Wiedemann and Professor Nikolaus Pfanner of the University of Freiburg in Germany, and Professor Thomas Becker of the University of Bonn led a team that cracked the structure and function of the SAM complex.
study was recently published in the journal Nature under the title "Mitochondrial sorting and assembly machinery operates by β-barrels."
SAM complex usually consists of two β-barrel membrane protein sub-base called Sam50, the outer β of which are covered by two other sub-base Sam35 and Sam37.
the researchers found that although the SAM complex formed a β-barrel membrane protein, it contained only one Sam50.
the second β-barrel membrane protein sub-base functions as a flexible placeholder: it temporarily leaves the SAM complex to make room for the formation of the new β-barrel membrane protein.
this dynamic mechanism shows how the new β-barrel membrane protein matures to full size in the SAM complex and can only be released as a fully folded protein.
we can identify new principles for membrane protein formation that plays a vital role in our cells," explains Wiedemann, a researcher at the U.S. Department of Science and Technology.
" Reference: 1.Hironori Takeda et al. Mitochondrial sorting and assembly machinery operates by β-barrel switching. Nature, 2021, doi:10.1038/s41586-020-03113-7. 2.The basis for mitochondria, essential cellular powerhouses