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Translocation of Proteins into the Mitochondria

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Mitochondria

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Related Experiment Video

Updated: Jun 28, 2025

Measurement of Protein Import Capacity of Skeletal Muscle Mitochondria

Measurement of Protein Import Capacity of Skeletal Muscle Mitochondria

Published on: January 7, 2022

Mitochondria function in cytoplasmic FeS protein biogenesis.

Andrew Dancis¹, Ashutosh K Pandey¹, Debkumar Pain¹

¹Department of Pharmacology, Physiology and Neuroscience, New Jersey Medical School, Rutgers University, Newark, NJ 07103, USA.

Biochimica Et Biophysica Acta. Molecular Cell Research

|April 19, 2024

Summary

Iron-sulfur (FeS) clusters are vital for cellular functions. This study reveals a mitochondrial intermediate (X-S) exported by Atm1, essential for cytoplasmic FeS protein assembly, explaining upstream mitochondrial control.

Keywords:

(Fe-S)(int)Atm1 Cytoplasm FeS cluster trafficking FeS proteins Glutaredoxin Glutathione Mitochondria X-S

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Measurement of Protein Import Capacity of Skeletal Muscle Mitochondria

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Analysis of the Expression and Complexes Assembly of the Mitochondrial Respiratory Chain Proteins in the Fission Yeast Schizosaccharomyces pombe

Analysis of the Expression and Complexes Assembly of the Mitochondrial Respiratory Chain Proteins in the Fission Yeast Schizosaccharomyces pombe

Published on: May 2, 2025

Area of Science:

Biochemistry
Molecular Biology
Cell Biology

Background:

Iron-sulfur (FeS) clusters are essential cofactors for numerous proteins involved in critical cellular processes.
The biogenesis of FeS clusters involves complex, conserved machinery, with distinct mitochondrial (ISC) and cytoplasmic (CIA) pathways in eukaryotes.
A unique mitochondrial intermediate (X-S) is proposed to link the ISC and CIA pathways.

Purpose of the Study:

To present genetic and biochemical evidence supporting the role of a mitochondrial FeS intermediate (X-S) exported by Atm1.
To review structural insights into the Atm1 transporter and its role in FeS cluster biogenesis.
To elucidate the compartmental roles of glutathione in cellular FeS cluster assembly.

Main Methods:

Genetic analysis of FeS cluster biogenesis pathways.
Biochemical assays to characterize FeS cluster assembly and intermediates.
Review of structural data for the mitochondrial ABC transporter Atm1.
Analysis of cellular phenotypes resulting from mutations or depletion of ISC machinery components and Atm1.

Main Results:

Evidence presented supports the existence and function of the X-S intermediate in FeS cluster biogenesis.
Structural reviews highlight the transport mechanism of Atm1.
Glutathione's critical role in compartmentalized FeS cluster assembly is emphasized.
Deficiency in mitochondrial ISC machinery or Atm1 leads to both mitochondrial and cytoplasmic FeS cluster deficits, confirming epistasis.

Conclusions:

The mitochondrial ISC machinery produces an intermediate (X-S) exported by Atm1, which is crucial for cytoplasmic FeS protein assembly.
This mechanism explains the observed epistasis between mitochondrial and cytoplasmic FeS biogenesis pathways.
The findings provide a comprehensive view of eukaryotic FeS cluster biogenesis, highlighting inter-compartmental coordination.