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.

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.

Related Concept Videos

Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death.  Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Energy to Drive Translocation01:37

Energy to Drive Translocation

Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
The Inner Mitochondrial Membrane01:28

The Inner Mitochondrial Membrane

The inner mitochondrial membrane is the primary site of ATP synthesis. The inner membrane domain that forms a smooth layer adjacent to the outer membrane is called the inner boundary membrane. This domain contains membrane transporters that drive metabolites in and out of the mitochondria.  In contrast, the inner membrane network that invaginates into the matrix space is called the cristae membrane. This domain accounts for principle mitochondrial function as it accommodates the protein...
The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...