ArticleThe EMBO journal2000
Recognition of preproteins by the isolated TOM complex of mitochondria.
Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 91 citations in OpenAlex.
- Molecular mechanism by which SARS-CoV-2 Orf9b suppresses the Tom70-Hsp90 interaction to evade innate immunity.Science advances · 2026Article
- Molecular mechanism by which SARS-CoV-2 Orf9b suppresses the Tom70-Hsp90 interaction to evade innate immunity.bioRxiv : the preprint server for biology · 2025Article
- A protein-specific priority code in presequences determines the efficiency of mitochondrial protein import.PLoS biology · 2025Article
- Two mitochondrial HMG-box proteins, Cim1 and Abf2, antagonistically regulate mtDNA copy number in Saccharomyces cerevisiae.Nucleic acids research · 2023Article
- Mitochondrial protein translocation machinery: From TOM structural biogenesis to functional regulation.The Journal of biological chemistry · 2022Review
- The Diversity of the Mitochondrial Outer Membrane Protein Import Channels: Emerging Targets for Modulation.Molecules (Basel, Switzerland) · 2021Review
- Targeting Mitochondrial Protein Expression as a Future Approach for Cancer Therapy.Frontiers in oncology · 2021Review
- Post-transcriptional control of mitochondrial protein composition in changing environmental conditions.Biochemical Society transactions · 2020Review
- How lipids modulate mitochondrial protein import.Journal of bioenergetics and biomembranes · 2016Review
- Capitalizing Resolving Power of Density Gradient Ultracentrifugation by Freezing and Precisely Slicing Centrifuged Solution: Enabling Identification of Complex Proteins from Mitochondria by Matrix Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry.Journal of analytical methods in chemistry · 2016Article
- A discrete pathway for the transfer of intermembrane space proteins across the outer membrane of mitochondria.Molecular biology of the cell · 2014Article
- OM14 is a mitochondrial receptor for cytosolic ribosomes that supports co-translational import into mitochondria.Nature communications · 2014Article
- Presequence recognition by the tom40 channel contributes to precursor translocation into the mitochondrial matrix.Molecular and cellular biology · 2014Article
- Protein translocation through Tom40: kinetics of peptide release.Biophysical journal · 2012Article
- Assembly of the mitochondrial protein import channel: role of Tom5 in two-stage interaction of Tom40 with the SAM complex.Molecular biology of the cell · 2010Article
- Interactions of mitochondrial presequence peptides with the mitochondrial outer membrane preprotein translocase TOM.Biophysical journal · 2010Article
- Quaternary structure of the mitochondrial TIM23 complex reveals dynamic association between Tim23p and other subunits.Molecular biology of the cell · 2008Article
- A cooperative action of the ATP-dependent import motor complex and the inner membrane potential drives mitochondrial preprotein import.Molecular and cellular biology · 2007Article
- The N-terminal domain of Tob55 has a receptor-like function in the biogenesis of mitochondrial beta-barrel proteins.The Journal of cell biology · 2007Article
- A cryptic matrix targeting signal of the yeast ADP/ATP carrier normally inserted by the TIM22 complex is recognized by the TIM23 machinery.The Biochemical journal · 2005Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A multisubunit complex in the mitochondrial outer membrane, the TOM complex, mediates targeting and membrane translocation of nuclear-encoded preproteins. We have isolated the TOM holo complex, containing the preprotein receptor components Tom70 and Tom20, and the TOM core complex, which lacks these receptors. The interaction of recombinant mitochondrial preproteins with both types of soluble TOM complex was analyzed. Preproteins bound efficiently in a specific manner to the isolated complexes in the absence of chaperones and lipids in a bilayer structure. Using fluorescence correlation spectroscopy, a dissociation constant in the nanomolar range was determined. The affinity was lower when the preprotein was stabilized in its folded conformation. Following the initial binding, the presequence was transferred into the translocation pore in a step that required unfolding of the mature part of the preprotein. This translocation step was also mediated by protease-treated TOM holo complex, which contains almost exclusively Tom40. Thus, the TOM core complex, consisting of Tom40, Tom22, Tom6 and Tom7, is a molecular machine that can recognize and partially translocate mitochondrial precursor proteins.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.