%0 Journal Article %1 qiuCouplingMitochondrialImport2013a %A Qiu, Jian %A Wenz, Lena-Sophie %A Zerbes, Ralf M. %A Oeljeklaus, Silke %A Bohnert, Maria %A Stroud, David A. %A Wirth, Christophe %A Ellenrieder, Lars %A Thornton, Nicolas %A Kutik, Stephan %A Wiese, Sebastian %A Schulze-Specking, Agnes %A Zufall, Nicole %A Chacinska, Agnieszka %A Guiard, Bernard %A Hunte, Carola %A Warscheid, Bettina %A van der Laan, Martin %A Pfanner, Nikolaus %A Wiedemann, Nils %A Becker, Thomas %C United States %D 2013 %J Cell %K *Protein Folding,Protein Membrane Proteins/chemistry/*metabolism,Mutation,Porins/chemistry/metabolism,Protein Proteins/chemistry/genetics/*metabolism,Saccharomyces Proteins/genetics/*metabolism,Mitochondrial Secondary,Saccharomyces Structure Transport Transport,Mitochondria/*metabolism,Mitochondrial cerevisiae cerevisiae/*metabolism,to_read %N 3 %P 596--608 %R 10.1016/j.cell.2013.06.033 %T Coupling of Mitochondrial Import and Export Translocases by Receptor-Mediated Supercomplex Formation. %V 154 %X The mitochondrial outer membrane harbors two protein translocases that are essential for cell viability: the translocase of the outer mitochondrial membrane (TOM) and the sorting and assembly machinery (SAM). The precursors of $\beta$-barrel proteins use both translocases-TOM for import to the intermembrane space and SAM for export into the outer membrane. It is unknown if the translocases cooperate and where the $\beta$-barrel of newly imported proteins is formed. We established a position-specific assay for monitoring $\beta$-barrel formation in vivo and in organello and demonstrated that the $\beta$-barrel was formed and membrane inserted while the precursor was bound to SAM. $\beta$-barrel formation was inhibited by SAM mutants and, unexpectedly, by mutants of the central import receptor, Tom22. We show that the cytosolic domain of Tom22 links TOM and SAM into a supercomplex, facilitating precursor transfer on the intermembrane space side. Our study reveals receptor-mediated coupling of import and export translocases as a means of precursor channeling.

@article{qiuCouplingMitochondrialImport2013a, abstract = {The mitochondrial outer membrane harbors two protein translocases that are essential for cell viability: the translocase of the outer mitochondrial membrane (TOM) and the sorting and assembly machinery (SAM). The precursors of {$\beta$}-barrel proteins use both translocases-TOM for import to the intermembrane space and SAM for export into the outer membrane. It is unknown if the translocases cooperate and where the {$\beta$}-barrel of newly imported proteins is formed. We established a position-specific assay for monitoring {$\beta$}-barrel formation in vivo and in organello and demonstrated that the {$\beta$}-barrel was formed and membrane inserted while the precursor was bound to SAM. {$\beta$}-barrel formation was inhibited by SAM mutants and, unexpectedly, by mutants of the central import receptor, Tom22. We show that the cytosolic domain of Tom22 links TOM and SAM into a supercomplex, facilitating precursor transfer on the intermembrane space side. Our study reveals receptor-mediated coupling of import and export translocases as a means of precursor channeling.}, added-at = {2024-05-17T13:01:35.000+0200}, address = {United States}, author = {Qiu, Jian and Wenz, Lena-Sophie and Zerbes, Ralf M. and Oeljeklaus, Silke and Bohnert, Maria and Stroud, David A. and Wirth, Christophe and Ellenrieder, Lars and Thornton, Nicolas and Kutik, Stephan and Wiese, Sebastian and {Schulze-Specking}, Agnes and Zufall, Nicole and Chacinska, Agnieszka and Guiard, Bernard and Hunte, Carola and Warscheid, Bettina and {van der Laan}, Martin and Pfanner, Nikolaus and Wiedemann, Nils and Becker, Thomas}, biburl = {https://www.bibsonomy.org/bibtex/284c956a5c8741acdead8c2350d355e38/warscheidlab}, copyright = {Copyright {\copyright} 2013 Elsevier Inc. All rights reserved.}, doi = {10.1016/j.cell.2013.06.033}, interhash = {4fc5231511a0e1d69fb5e018394d185d}, intrahash = {84c956a5c8741acdead8c2350d355e38}, issn = {1097-4172 0092-8674}, journal = {Cell}, keywords = {*Protein Folding,Protein Membrane Proteins/chemistry/*metabolism,Mutation,Porins/chemistry/metabolism,Protein Proteins/chemistry/genetics/*metabolism,Saccharomyces Proteins/genetics/*metabolism,Mitochondrial Secondary,Saccharomyces Structure Transport Transport,Mitochondria/*metabolism,Mitochondrial cerevisiae cerevisiae/*metabolism,to_read}, langid = {english}, month = aug, number = 3, pages = {596--608}, pmid = {23911324}, timestamp = {2024-05-17T13:01:35.000+0200}, title = {Coupling of Mitochondrial Import and Export Translocases by Receptor-Mediated Supercomplex Formation.}, volume = 154, year = 2013 }