The majority of mitochondrial proteins are synthesized with amino-terminal signal sequences. The presequence translocase of the inner membrane (TIM23 complex) mediates the import of these preproteins. The essential TIM23 core complex closely cooperates with partner protein complexes like the presequence translocase-associated import motor and the respiratory chain. The inner mitochondrial membrane also contains a large number of metabolite carriers, but their association with preprotein translocases has been controversial. We performed a comprehensive analysis of the TIM23 interactome based on stable isotope labeling with amino acids in cell culture. Subsequent biochemical studies on identified partner proteins showed that the mitochondrial ADP/ATP carrier associates with the membrane-embedded core of the TIM23 complex in a stoichiometric manner, revealing an unexpected connection of mitochondrial protein biogenesis to metabolite transport. Our data indicate that direct TIM23-AAC coupling may support preprotein import into mitochondria when respiratory activity is low.
%0 Journal Article
%1 mehnertMitochondrialADPATP2014
%A Mehnert, Carola S.
%A Rampelt, Heike
%A Gebert, Michael
%A Oeljeklaus, Silke
%A Schrempp, Sandra G.
%A Kochbeck, Lioba
%A Guiard, Bernard
%A Warscheid, Bettina
%A van der Laan, Martin
%C United States
%D 2014
%J The Journal of biological chemistry
%K Carrier,Mitochondria,Mitochondrial Chain,Saccharomyces Complex Complex,to_read Complexes/genetics/*metabolism,Protein Import Import,Mitochondrial Membranes/*metabolism,Mitochondrial Metabolism,Membrane Precursor Protein Protein,Membrane Proteins,Mitochondrial Proteins/genetics/*metabolism,Metabolite Proteins/genetics/*metabolism,Multiprotein Proteins/genetics/*metabolism,Saccharomyces Translocation,Protein Transport Transport/physiology,Respiratory cerevisiae cerevisiae/genetics/*metabolism,SILAC,TIM23 energy
%N 39
%P 27352--27362
%R 10.1074/jbc.M114.556498
%T The Mitochondrial ADP/ATP Carrier Associates with the Inner Membrane Presequence Translocase in a Stoichiometric Manner.
%V 289
%X The majority of mitochondrial proteins are synthesized with amino-terminal signal sequences. The presequence translocase of the inner membrane (TIM23 complex) mediates the import of these preproteins. The essential TIM23 core complex closely cooperates with partner protein complexes like the presequence translocase-associated import motor and the respiratory chain. The inner mitochondrial membrane also contains a large number of metabolite carriers, but their association with preprotein translocases has been controversial. We performed a comprehensive analysis of the TIM23 interactome based on stable isotope labeling with amino acids in cell culture. Subsequent biochemical studies on identified partner proteins showed that the mitochondrial ADP/ATP carrier associates with the membrane-embedded core of the TIM23 complex in a stoichiometric manner, revealing an unexpected connection of mitochondrial protein biogenesis to metabolite transport. Our data indicate that direct TIM23-AAC coupling may support preprotein import into mitochondria when respiratory activity is low.
@article{mehnertMitochondrialADPATP2014,
abstract = {The majority of mitochondrial proteins are synthesized with amino-terminal signal sequences. The presequence translocase of the inner membrane (TIM23 complex) mediates the import of these preproteins. The essential TIM23 core complex closely cooperates with partner protein complexes like the presequence translocase-associated import motor and the respiratory chain. The inner mitochondrial membrane also contains a large number of metabolite carriers, but their association with preprotein translocases has been controversial. We performed a comprehensive analysis of the TIM23 interactome based on stable isotope labeling with amino acids in cell culture. Subsequent biochemical studies on identified partner proteins showed that the mitochondrial ADP/ATP carrier associates with the membrane-embedded core of the TIM23 complex in a stoichiometric manner, revealing an unexpected connection of mitochondrial protein biogenesis to metabolite transport. Our data indicate that direct TIM23-AAC coupling may support preprotein import into mitochondria when respiratory activity is low.},
added-at = {2024-05-17T13:01:35.000+0200},
address = {United States},
author = {Mehnert, Carola S. and Rampelt, Heike and Gebert, Michael and Oeljeklaus, Silke and Schrempp, Sandra G. and Kochbeck, Lioba and Guiard, Bernard and Warscheid, Bettina and {van der Laan}, Martin},
biburl = {https://www.bibsonomy.org/bibtex/29d19fb6a710df2201e20149407b45913/warscheidlab},
copyright = {{\copyright} 2014 by The American Society for Biochemistry and Molecular Biology, Inc.},
doi = {10.1074/jbc.M114.556498},
interhash = {b25345abf9518285942c3243368f0285},
intrahash = {9d19fb6a710df2201e20149407b45913},
issn = {1083-351X 0021-9258},
journal = {The Journal of biological chemistry},
keywords = {Carrier,Mitochondria,Mitochondrial Chain,Saccharomyces Complex Complex,to_read Complexes/genetics/*metabolism,Protein Import Import,Mitochondrial Membranes/*metabolism,Mitochondrial Metabolism,Membrane Precursor Protein Protein,Membrane Proteins,Mitochondrial Proteins/genetics/*metabolism,Metabolite Proteins/genetics/*metabolism,Multiprotein Proteins/genetics/*metabolism,Saccharomyces Translocation,Protein Transport Transport/physiology,Respiratory cerevisiae cerevisiae/genetics/*metabolism,SILAC,TIM23 energy},
langid = {english},
month = sep,
number = 39,
pages = {27352--27362},
pmcid = {PMC4175365},
pmid = {25124039},
timestamp = {2024-05-17T13:01:35.000+0200},
title = {The Mitochondrial {{ADP}}/{{ATP}} Carrier Associates with the Inner Membrane Presequence Translocase in a Stoichiometric Manner.},
volume = 289,
year = 2014
}