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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,...

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...

Protein Transport into the Inner Mitochondrial Membrane

Protein Transport into the Inner Mitochondrial Membrane

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...

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...

Transfer RNA Synthesis

Transfer RNA Synthesis

One of the unique features of tRNA is the presence of modified bases. In some tRNAs, modified bases account for nearly 20% of the total bases in the molecule. Altogether, these unusual bases protect the tRNA from enzymatic degradation by RNases.
Each of these chemical modifications is carried by a specific enzyme, post-transcription. All of these enzymes have unique base and site-specificity. Methylation, the most common chemical modification, is carried by at least nine different enzymes, with...

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...

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Related Experiment Video

Updated: Feb 25, 2026

Discrimintion and Mapping of the Primary and Processed Transcripts in Maize Mitochondrion Using a Circular RT-PCR-based Strategy

Discrimintion and Mapping of the Primary and Processed Transcripts in Maize Mitochondrion Using a Circular RT-PCR-based Strategy

Published on: July 29, 2019

TDP-43 stabilises the processing intermediates of mitochondrial transcripts.

Keiichi Izumikawa^1,2, Yuko Nobe^2,3, Harunori Yoshikawa^1,2,4

¹Global Innovation Research Organizations, Tokyo University of Agriculture and Technology, 3-5-8 Saiwai-cho, Fuchu, Tokyo, 183-8509, Japan.

Scientific Reports

|August 11, 2017

Summary

This summary is machine-generated.

Trans-activating response region DNA-binding protein 43 (TDP-43) maintains mitochondrial homeostasis by regulating mitochondrial RNA processing. TDP-43 deficiency impairs mitochondrial function, suggesting a novel role in amyotrophic lateral sclerosis pathogenesis.

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Area of Science:

Mitochondrial biology
Neurodegenerative diseases
Molecular genetics

Background:

Amyotrophic lateral sclerosis (ALS) is linked to TDP-43 gene mutations.
Mitochondrial dysfunction is implicated in TDP-43-related ALS pathogenesis.
The role of wild-type TDP-43 in mitochondria remains unclear.

Purpose of the Study:

To investigate the function of TDP-43 within mitochondria.
To elucidate the role of TDP-43 in mitochondrial RNA processing and homeostasis.

Main Methods:

Mitochondrial protein localization studies.
RNA binding assays using mitochondrial tRNAs and mtDNA.
Analysis of mitochondrial transcript processing intermediates.
Assessment of mitochondrial function under varying TDP-43 expression levels.

Main Results:

TDP-43 localizes to mitochondria and binds to mitochondrial tRNAs and L-strand mtDNA transcripts.
Overexpression of TDP-43 stabilizes mitochondrial transcript processing intermediates.
TDP-43 deficiency impairs mitochondrial function and reduces processing intermediates.

Conclusions:

TDP-43 plays a novel role in maintaining mitochondrial homeostasis.
TDP-43 regulates the processing of mitochondrial transcripts.
Dysregulation of TDP-43's mitochondrial function may contribute to ALS pathogenesis.