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ATP Synthase: Mechanism

ATP Synthase: Mechanism

In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...

ATP Synthase: Structure

ATP Synthase: Structure

ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...

Chemiosmosis

Chemiosmosis

Oxidative phosphorylation is a highly efficient process that generates large amounts of adenosine triphosphate (ATP), the basic unit of energy that drives many cellular processes. Oxidative phosphorylation involves two processes— the electron transport chain and chemiosmosis.
Electron Transport Chain
The electron transport chain involves a series of protein complexes on the inner mitochondrial membrane that undergo a series of redox reactions. At the end of this chain, the electrons...

Energy to Drive Translocation

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 Membrane

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...

Mitochondrial Protein Sorting

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...

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Related Experiment Video

Updated: May 12, 2025

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

Published on: September 14, 2014

Mitochondrial calpain-1 truncates ATP synthase beta subunit.

Yusaku Chukai¹, Nanami Furukawa¹, On Kosegawa²

¹Laboratory of Cell Biochemistry, Department of Life Sciences, Faculty of Agriculture, Iwate University, Morioka, Iwate, Japan; Laboratory of Cell Biochemistry, Department of Biological Science, Graduate School of Science and Engineering, Iwate University, Morioka, Iwate, Japan.

Biochemical and Biophysical Research Communications

|April 22, 2025

Summary

Mitochondrial calpain-1 cleaves ATP5B, a key protein in cellular energy production. This cleavage disrupts ATP synthesis, contributing to mitochondrial dysfunction and apoptosis.

Keywords:

ATP5B Calpain-1 Mitochondria

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Last Updated: May 12, 2025

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

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Published on: September 14, 2014

F1FO ATPase Vesicle Preparation and Technique for Performing Patch Clamp Recordings of Submitochondrial Vesicle Membranes

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Published on: May 4, 2013

Assessment of Open Probability of the Mitochondrial Permeability Transition Pore in the Setting of Coenzyme Q Excess

Assessment of Open Probability of the Mitochondrial Permeability Transition Pore in the Setting of Coenzyme Q Excess

Published on: June 1, 2022

Area of Science:

Biochemistry
Cell Biology
Mitochondrial Biology

Background:

Calpains are calcium-dependent proteases regulating cellular functions.
Mitochondrial calpain-1 contributes to apoptosis by cleaving substrates.
Identifying mitochondrial calpain-1 substrates is crucial for understanding its role.

Purpose of the Study:

To identify novel substrates of mitochondrial calpain-1.
To investigate the functional consequences of calpain-1 cleavage on its substrates.

Main Methods:

Bioinformatics screening of mitochondrial proteins.
Two-dimensional gel electrophoresis.
In vitro biochemical assays using recombinant proteins and inhibitors.

Main Results:

ATP5B was identified as a novel substrate of mitochondrial calpain-1.
Calpain inhibitors prevented ATP5B truncation.
Calpain-1 directly cleaved ATP5B, producing a distinct fragment.
Cleavage may impair ATP5B interaction with ATP5A1, affecting ATP production.

Conclusions:

ATP5B is a direct substrate of mitochondrial calpain-1.
Calpain-1-mediated cleavage of ATP5B contributes to mitochondrial dysfunction.
This finding offers new insights into the mechanisms of mitochondrial dysfunction.