%0 Journal Article %1 opalinskiRecruitmentCytosolicJProteins2018a %A Opaliński, Łukasz %A Song, Jiyao %A Priesnitz, Chantal %A Wenz, Lena-Sophie %A Oeljeklaus, Silke %A Warscheid, Bettina %A Pfanner, Nikolaus %A Becker, Thomas %C United States %D 2018 %J Cell reports %K *Protein Biosynthesis,Carrier Complex Domains,protein Import Precursor Protein Proteins,Mitochondrial Proteins/*metabolism,Cytosol/*metabolism,cytosolic Proteins/*metabolism,Protein Proteins/chemistry/metabolism,Saccharomyces Specificity,to_read,TOM cerevisiae cerevisiae/*metabolism,Substrate chaperones,J-proteins,mitochondria,Mitochondria/*metabolism,Mitochondrial complex targeting,Saccharomyces %N 8 %P 2036-2043.e5 %R 10.1016/j.celrep.2018.10.083 %T Recruitment of Cytosolic J-Proteins by TOM Receptors Promotes Mitochondrial Protein Biogenesis. %V 25 %X Mitochondria possess elaborate machineries for the import of proteins from the cytosol. Cytosolic factors like Hsp70 chaperones and their co-chaperones, the J-proteins, guide proteins to the mitochondrial surface. The translocase of the mitochondrial outer membrane (TOM) forms the entry gate for preproteins. How the proteins are delivered to mitochondrial preprotein receptors is poorly understood. We identify the cytosolic J-protein Xdj1 as a specific interaction partner of the central receptor Tom22. Tom22 recruits Xdj1 to the mitochondrial surface to promote import of preproteins and assembly of the TOM complex. Additionally, we find that the receptor Tom70 binds a different cytosolic J-protein, Djp1. Our findings suggest that cytosolic J-proteins target distinct TOM receptors and promote the biogenesis of mitochondrial proteins.

@article{opalinskiRecruitmentCytosolicJProteins2018a, abstract = {Mitochondria possess elaborate machineries for the import of proteins from the cytosol. Cytosolic factors like Hsp70 chaperones and their co-chaperones, the J-proteins, guide proteins to the mitochondrial surface. The translocase of the mitochondrial outer membrane (TOM) forms the entry gate for preproteins. How the proteins are delivered to mitochondrial preprotein receptors is poorly understood. We identify the cytosolic J-protein Xdj1 as a specific interaction partner of the central receptor Tom22. Tom22 recruits Xdj1 to the mitochondrial surface to promote import of preproteins and assembly of the TOM complex. Additionally, we find that the receptor Tom70 binds a different cytosolic J-protein, Djp1. Our findings suggest that cytosolic J-proteins target distinct TOM receptors and promote the biogenesis of mitochondrial proteins.}, added-at = {2024-05-17T13:01:35.000+0200}, address = {United States}, author = {Opali{\'n}ski, {\L}ukasz and Song, Jiyao and Priesnitz, Chantal and Wenz, Lena-Sophie and Oeljeklaus, Silke and Warscheid, Bettina and Pfanner, Nikolaus and Becker, Thomas}, biburl = {https://www.bibsonomy.org/bibtex/2390c6b381e21e9e4e2097f28ab01dad6/warscheidlab}, copyright = {Copyright {\copyright} 2018 The Author(s). Published by Elsevier Inc. All rights reserved.}, doi = {10.1016/j.celrep.2018.10.083}, interhash = {82db330ad3502cdd432456d0c6e623f6}, intrahash = {390c6b381e21e9e4e2097f28ab01dad6}, issn = {2211-1247}, journal = {Cell reports}, keywords = {*Protein Biosynthesis,Carrier Complex Domains,protein Import Precursor Protein Proteins,Mitochondrial Proteins/*metabolism,Cytosol/*metabolism,cytosolic Proteins/*metabolism,Protein Proteins/chemistry/metabolism,Saccharomyces Specificity,to_read,TOM cerevisiae cerevisiae/*metabolism,Substrate chaperones,J-proteins,mitochondria,Mitochondria/*metabolism,Mitochondrial complex targeting,Saccharomyces}, langid = {english}, month = nov, number = 8, pages = {2036-2043.e5}, pmcid = {PMC6280124}, pmid = {30463002}, timestamp = {2024-05-17T13:01:35.000+0200}, title = {Recruitment of {{Cytosolic J-Proteins}} by {{TOM Receptors Promotes Mitochondrial Protein Biogenesis}}.}, volume = 25, year = 2018 }