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Mitochondrial Precursor Proteins

Mitochondrial Precursor Proteins

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 precursors...

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...

Translocation of Proteins into the Mitochondria

Translocation of Proteins into the Mitochondria

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,...

Electron Transport Chain: Complex I and II

Electron Transport Chain: Complex I and II

The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
ROS generation is regulated and maintained at moderate levels necessary...

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...

Porin Insertion in the Outer Mitochondrial Membrane

Porin Insertion in the Outer Mitochondrial Membrane

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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Related Experiment Video

Updated: Jun 26, 2026

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Published on: August 10, 2021

C-terminal binding protein maintains mitochondrial activities.

J H Kim¹, H D Youn

¹National Research Laboratory for Metabolic Checkpoint, Department of Biomedical Sciences & Biochemistry and Molecular Biology, Cancer Research Institute, Seoul National University College of Medicine, Seoul 110-799, Republic of Korea.

Cell Death and Differentiation

|January 13, 2009

Summary

C-terminal binding protein (CtBP) acts as a metabolic sensor, repressing Bax transcription under high glucose conditions. Glucose withdrawal disrupts this, impacting mitochondrial function and morphology.

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Area of Science:

Cell Biology
Molecular Biology
Metabolism

Background:

Mitochondria are vital for cellular energy and apoptosis.
C-terminal binding protein (CtBP) is a metabolic sensor, but its role in metabolic stress-induced gene transcription is unknown.

Purpose of the Study:

To investigate if CtBP controls gene transcription in response to metabolic stress.
To elucidate the mechanism by which CtBP regulates mitochondrial activity.

Main Methods:

Analysis of CtBP binding to the Bax promoter under varying glucose conditions.
Assessment of histone modifications at the Bax promoter.
CtBP knockout and ectopic expression studies.
Evaluation of mitochondrial morphology and function.

Main Results:

CtBP represses Bcl-2-associated X protein (Bax) transcription via E-box binding in glucose-rich media.
Glucose withdrawal causes CtBP dissociation from the Bax promoter and alters histone codes.
CtBP knockout leads to increased Bax transcription, impaired mitochondrial morphology, and reduced activity.
Restoration of CtBP or Bax knockdown rescues mitochondrial function in knockout cells.

Conclusions:

CtBP functions as a metabolic sensor, maintaining mitochondrial activity by repressing Bax transcription.
Intracellular energy levels are linked to gene transcription regulating mitochondrial morphology and function.