%0 Journal Article %1 kaserOuterMembraneProtein2016 %A Käser, Sandro %A Oeljeklaus, Silke %A Týc, Jirí %A Vaughan, Sue %A Warscheid, Bettina %A Schneider, André %C United States %D 2016 %J Proceedings of the National Academy of Sciences of the United States of America %K Acid Acid,to_read,Trypanosoma Amino Complex Homology Import Interference,Sequence Line,DNA Membrane Mitochondrial/genetics,mitochondria,mitochondrial Mitochondrial/genetics/*metabolism,DNA Precursor Protein Proteins,Mitochondrial Proteins/genetics/*metabolism,Mitochondrial Proteins/genetics/*metabolism,RNA Proteins/genetics/*metabolism,protein Proteins/genetics/metabolism,Cell Protozoan/genetics/metabolism,evolution,Flagella/metabolism,Genome Sequence,Carrier Transport Transport/genetics,Protozoan brucei brucei/cytology/genetics/*metabolism,trypanosomes genome,Mitochondrial import,Protein %N 31 %P E4467-4475 %R 10.1073/pnas.1605497113 %T Outer Membrane Protein Functions as Integrator of Protein Import and DNA Inheritance in Mitochondria. %V 113 %X Trypanosomatids are one of the earliest diverging eukaryotes that have fully functional mitochondria. pATOM36 is a trypanosomatid-specific essential mitochondrial outer membrane protein that has been implicated in protein import. Changes in the mitochondrial proteome induced by ablation of pATOM36 and in vitro assays show that pATOM36 is required for the assembly of the archaic translocase of the outer membrane (ATOM), the functional analog of the TOM complex in other organisms. Reciprocal pull-down experiments and immunofluorescence analyses demonstrate that a fraction of pATOM36 interacts and colocalizes with TAC65, a previously uncharacterized essential component of the tripartite attachment complex (TAC). The TAC links the single-unit mitochondrial genome to the basal body of the flagellum and mediates the segregation of the replicated mitochondrial genomes. RNAi experiments show that pATOM36, in line with its dual localization, is not only essential for ATOM complex assembly but also for segregation of the replicated mitochondrial genomes. However, the two functions are distinct, as a truncated version of pATOM36 lacking the 75 C-terminal amino acids can rescue kinetoplast DNA missegregation but not the lack of ATOM complex assembly. Thus, pATOM36 has a dual function and integrates mitochondrial protein import with mitochondrial DNA inheritance.

@article{kaserOuterMembraneProtein2016, abstract = {Trypanosomatids are one of the earliest diverging eukaryotes that have fully functional mitochondria. pATOM36 is a trypanosomatid-specific essential mitochondrial outer membrane protein that has been implicated in protein import. Changes in the mitochondrial proteome induced by ablation of pATOM36 and in vitro assays show that pATOM36 is required for the assembly of the archaic translocase of the outer membrane (ATOM), the functional analog of the TOM complex in other organisms. Reciprocal pull-down experiments and immunofluorescence analyses demonstrate that a fraction of pATOM36 interacts and colocalizes with TAC65, a previously uncharacterized essential component of the tripartite attachment complex (TAC). The TAC links the single-unit mitochondrial genome to the basal body of the flagellum and mediates the segregation of the replicated mitochondrial genomes. RNAi experiments show that pATOM36, in line with its dual localization, is not only essential for ATOM complex assembly but also for segregation of the replicated mitochondrial genomes. However, the two functions are distinct, as a truncated version of pATOM36 lacking the 75 C-terminal amino acids can rescue kinetoplast DNA missegregation but not the lack of ATOM complex assembly. Thus, pATOM36 has a dual function and integrates mitochondrial protein import with mitochondrial DNA inheritance.}, added-at = {2024-05-17T13:01:35.000+0200}, address = {United States}, author = {K{\"a}ser, Sandro and Oeljeklaus, Silke and T{\'y}{\v c}, Ji{\v r}{\'i} and Vaughan, Sue and Warscheid, Bettina and Schneider, Andr{\'e}}, biburl = {https://www.bibsonomy.org/bibtex/2b485759af46ce7bdc76bdd20f77ea24d/warscheidlab}, doi = {10.1073/pnas.1605497113}, interhash = {2002ae1d8ce359b3f34a9c6ea4997c0d}, intrahash = {b485759af46ce7bdc76bdd20f77ea24d}, issn = {1091-6490 0027-8424}, journal = {Proceedings of the National Academy of Sciences of the United States of America}, keywords = {Acid Acid,to_read,Trypanosoma Amino Complex Homology Import Interference,Sequence Line,DNA Membrane Mitochondrial/genetics,mitochondria,mitochondrial Mitochondrial/genetics/*metabolism,DNA Precursor Protein Proteins,Mitochondrial Proteins/genetics/*metabolism,Mitochondrial Proteins/genetics/*metabolism,RNA Proteins/genetics/*metabolism,protein Proteins/genetics/metabolism,Cell Protozoan/genetics/metabolism,evolution,Flagella/metabolism,Genome Sequence,Carrier Transport Transport/genetics,Protozoan brucei brucei/cytology/genetics/*metabolism,trypanosomes genome,Mitochondrial import,Protein}, langid = {english}, month = aug, number = 31, pages = {E4467-4475}, pmcid = {PMC4978248}, pmid = {27436903}, timestamp = {2024-05-17T13:01:35.000+0200}, title = {Outer Membrane Protein Functions as Integrator of Protein Import and {{DNA}} Inheritance in Mitochondria.}, volume = 113, year = 2016 }