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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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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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Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

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After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

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The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the...
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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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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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Related Experiment Video

Updated: Dec 3, 2025

Reconstitution of Msp1 Extraction Activity with Fully Purified Components
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Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Published on: August 10, 2021

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OMA1-An integral membrane protease?

Marcel V Alavi1

  • 1712 North Inc., QB3 Incubator at UC Berkeley, 130 Stanley Hall, #3220, Berkeley CA-94720, USA.

Biochimica Et Biophysica Acta. Proteins and Proteomics
|November 1, 2020
PubMed
Summary
This summary is machine-generated.

The mitochondrial protease OMA1, activated by stress, processes key proteins like DELE1 and OPA1. This review proposes OMA1 is an integral membrane protease, crucial for understanding cellular stress responses and diseases.

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Area of Science:

  • Mitochondrial biology
  • Protease biochemistry
  • Cellular stress response

Background:

  • OMA1 is a mitochondrial protease regulating signaling peptides (DELE1) and mitochondrial outer membrane permeabilization (OPA1).
  • OMA1 is activated by mitochondrial stress (e.g., loss of membrane potential, ROS) and implicated in diseases like cancer and neurodegeneration.
  • OMA1's structure, precise localization, and regulation remain largely uncharacterized.

Purpose of the Study:

  • To review the existing literature on OMA1 biochemistry and regulation.
  • To present a homology model of OMA1's active site.
  • To argue for OMA1's function as an integral membrane protease.

Main Methods:

  • Literature review focusing on OMA1 biochemistry.
  • Computational modeling: homology modeling of OMA1 active site (RMSD 0.9 Å, DALI Z-score 19.8).
  • Comparative analysis with related proteases (PARL, ZMPSTE24).

Main Results:

  • A homology model of OMA1's active site was generated, demonstrating high structural similarity.
  • Evidence suggests OMA1 functions as an integral membrane protease, not merely tethered.
  • OMA1's role in generating signaling peptides and its homology to ZMPSTE24 support its integral membrane nature.

Conclusions:

  • OMA1 is a critical mitochondrial protease involved in stress response and disease.
  • This review provides strong evidence for OMA1 being an integral membrane protease.
  • A refined understanding of OMA1 biochemistry will facilitate the development of targeted chemical probes and therapeutics.