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Updated: Aug 19, 2026

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
Published on: September 14, 2014
Role of Tom5 in maintaining the structural stability of the TOM complex of mitochondria
Simone Schmitt1, Uwe Ahting, Lutz Eichacker
1Adolf-Butenandt-Institut für Physiologische Chemie, Ludwig-Maximilians-Universität München, 81377 München, Germany.
Abstract:
Transport of nuclear encoded proteins into mitochondria is mediated by multisubunit translocation machineries in the outer and inner membranes of mitochondria. The TOM complex contains receptor and pore components that facilitate the recognition of preproteins and their transfer through the outer membrane. In addition, the complex contains a set of small proteins. Tom7 and Tom6 have been found in Neurospora and yeast, Tom5 has been found so far only in the latter organism. In the present study, we identified Neurospora Tom5 and analyzed its function in comparison to yeast Tom5, which has been proposed to play a role as a receptor-like component. Neurospora Tom5 crosses the outer membrane with its carboxyl terminus facing the intermembrane space like the other small Tom components. The temperature-sensitive growth phenotype of the yeast TOM5 deletion was rescued by overexpression of Neurospora Tom5. On the other hand, Neurospora cells deficient in tom5 did not exhibit any defect in growth. The structural stability of TOM complexes from cells devoid of Tom5 was significantly altered in yeast but not in Neurospora. The efficiency of protein import in Neurospora mitochondria was not affected by deletion of tom5, whereas in yeast it was reduced as compared with wild type. We conclude that the main role of Tom5, rather than being a receptor, is maintaining the structural integrity of the TOM complex.
Insights
Neurospora Tom5 protein was identified and found to maintain the structural integrity of the TOM complex, unlike its yeast counterpart which plays a role in protein import. This finding impacts our understanding of mitochondrial protein transport.
Area of Science:
- Mitochondrial biology
- Protein translocation
- Molecular cell biology
Background:
- Mitochondrial protein import relies on the TOM complex in the outer mitochondrial membrane.
- Small proteins like Tom7, Tom6, and Tom5 are components of the TOM complex.
- The precise function of Tom5, particularly in different organisms, remains incompletely understood.
Purpose of the Study:
- To identify and characterize Neurospora Tom5.
- To compare the function of Neurospora Tom5 with yeast Tom5.
- To elucidate the role of Tom5 in mitochondrial protein import and TOM complex stability.
Main Methods:
- Identification and analysis of Neurospora Tom5.
- Functional comparison using yeast TOM5 deletion and overexpression studies.
- Assessment of TOM complex structural stability and protein import efficiency in Neurospora and yeast.
Main Results:
- Neurospora Tom5 was identified and shown to localize with its carboxyl terminus in the intermembrane space.
- Overexpression of Neurospora Tom5 rescued the temperature-sensitive growth defect of yeast TOM5 deletion mutants.
- Deletion of tom5 in Neurospora did not affect growth or protein import efficiency, but altered TOM complex stability in yeast.
Conclusions:
- Tom5's primary role is maintaining TOM complex structural integrity, not acting as a receptor in protein import.
- Functional differences in Tom5 exist between Neurospora and yeast.
- The structural role of Tom5 is crucial for TOM complex stability, especially in yeast.
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