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Related Concept Videos

Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

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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,...
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Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

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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...
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Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

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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...
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Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

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Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial...
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Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

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Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on 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...
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Insertion of Multi-pass Transmembrane Proteins in the RER01:29

Insertion of Multi-pass Transmembrane Proteins in the RER

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The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
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A dynamic displacement mechanism drives protein import into mitochondria.

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Related Experiment Video

Updated: Sep 14, 2025

Preparation of the Mgm101 Recombination Protein by MBP-based Tagging Strategy
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The mammalian protein MTCH1 can function as an insertase.

Anna Roza Dimogkioka1, Anni Elias1, Doron Rapaport1

  • 1Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen 72076, Germany.

Journal of Cell Science
|July 24, 2025
PubMed
Summary

Mammalian MTCH1 protein can functionally replace yeast

Area of Science:

  • Mitochondrial biogenesis
  • Protein insertion
  • Outer mitochondrial membrane (OMM)

Background:

  • The outer mitochondrial membrane (OMM) is crucial for cellular functions, housing various proteins.
  • In yeast (Saccharomyces cerevisiae), the MIM complex (Mim1/Mim2) inserts α-helical proteins into the OMM.
  • Mammalian MTCH2 was identified as an OMM insertase, but MTCH1's role remained unclear.

Purpose of the Study:

  • To investigate the functional role of MTCH1 in protein insertion into the OMM.
  • To determine if MTCH1 or MTCH2 can functionally substitute for the yeast MIM complex.
  • To characterize MTCH1's contribution to mitochondrial biogenesis.

Main Methods:

  • Expression of mammalian MTCH1 and MTCH2 in yeast lacking MIM complex components (Mim1, Mim2).
Keywords:
InsertaseMIMMTCH1MTCH2MitochondriaOuter membrane

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Related Experiment Videos

Last Updated: Sep 14, 2025

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  • Assessment of yeast growth defects upon MIM complex deletion.
  • Analysis of MIM substrate biogenesis, TOM complex stability, and mitochondrial morphology.

    • Main Results:

    • MTCH1, but not MTCH2, rescued growth defects in yeast lacking the MIM complex.
    • MTCH1 restored the biogenesis of MIM substrates and the stability of the translocase of the outer membrane (TOM) complex.
    • MTCH1 also improved mitochondrial morphology in the absence of the native MIM complex.

    Conclusions:

    • MTCH1 possesses insertase activity and functions as a direct equivalent to the yeast MIM complex.
    • This functional conservation highlights MTCH1's essential role in OMM protein biogenesis.
    • MTCH1 is a functional homolog of the yeast MIM complex, despite lacking direct evolutionary linkage.