Related Experiment Video
Updated: Jun 19, 2026

Reconstitution of Msp1 Extraction Activity with Fully Purified Components
Published on: August 10, 2021
Genetic and functional interactions between the mitochondrial outer membrane proteins Tom6 and Sam37
Jovana Dukanovic1, Kai S Dimmer, Nathalie Bonnefoy
1Interfaculty Institute for Biochemistry, University of Tübingen, Hoppe-Seyler-Str. 4, 72076 Tübingen, Germany.
The mitochondrial SAM/TOB complex protein Sam37 interacts with Tom6, crucial for beta-barrel protein biogenesis. This interaction is vital for cell growth at higher temperatures, highlighting Sam37
Area of Science:
- Mitochondrial protein import and biogenesis
- Outer mitochondrial membrane protein insertion
- Protein complex interactions
Background:
- The TOM complex facilitates general mitochondrial protein entry.
- The SAM/TOB complex integrates beta-barrel proteins into the outer mitochondrial membrane.
- Sam37 is a core component of the SAM/TOB complex, essential for growth at elevated temperatures, but its function is unclear.
Purpose of the Study:
- To identify Sam37 interacting partners and elucidate its function.
- To investigate the functional relationship between Sam37 and the TOM complex.
Main Methods:
- Screening for multicopy suppressors of sam37 deletion (sam37Δ).
- Genetic interaction studies between SAM37 and TOM complex components.
- Analysis of cell viability and growth phenotypes under varying temperature conditions.
Main Results:
- Tom6, a small subunit of the TOM complex, was identified as a multicopy suppressor of sam37Δ.
- A tight genetic interaction was observed between Sam37 and Tom6; simultaneous deletion is lethal.
- Overexpression of Sam37 rescues the growth defect of tom6Δ, and Tom6 stabilizes Tom40, a key beta-barrel protein.
Conclusions:
- Sam37 is required for optimal growth at higher temperatures, likely by enhancing the biogenesis of the essential beta-barrel protein Tom40.
- The function of Sam37 in Tom40 biogenesis can be compensated by increased Tom40 stability mediated by Tom6.
- This study reveals a functional link between the SAM/TOB and TOM complexes, crucial for mitochondrial outer membrane protein biogenesis.
Related Concept Videos
Porin Insertion in the Outer Mitochondrial Membrane
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
Mitochondrial Protein Sorting
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
Structure of Porins
Translocation of Proteins into the Mitochondria
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,...
Protein Transport into the Inner Mitochondrial Membrane
Transport of mitochondrial precursors across the TIM23 channel is driven by...
Mitochondrial Membranes

