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Related Concept Videos

Mitochondrial Protein Sorting01:39

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 Mitochondria01:19

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 Precursor Proteins01:39

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...
Comparing Mitochondrial, Chloroplast, and Prokaryotic Genomes02:16

Comparing Mitochondrial, Chloroplast, and Prokaryotic Genomes

The present-day mitochondrial and chloroplast genomes have retained some of the characteristics of their ancestral prokaryotes and also have acquired new attributes during their evolution within eukaryotic cells. Like prokaryotic genomes, mitochondrial and chloroplast genomes neither bind with histone-like proteins nor show complex packaging into chromosome-like structures, as observed in eukaryotes. Unlike mitotic cell divisions observed in eukaryotic cells, mitochondria and chloroplasts...
Porin Insertion in the Outer Mitochondrial Membrane01:12

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...
Export of Mitochondrial and Chloroplast Genes02:19

Export of Mitochondrial and Chloroplast Genes

A eukaryotic cell can have up to three different types of genetic systems: nuclear, mitochondrial, and chloroplast. During evolution, organelles have exported many genes to the nucleus; this transfer is still ongoing in some plant species. Approximately 18% of the Arabidopsis thaliana nuclear genome is thought to be derived from the chloroplast’s cyanobacterial ancestor, and around 75% of the yeast genome derived from the mitochondria’s bacterial ancestor. This export has occurred irrespective...

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Related Experiment Video

Updated: Jun 23, 2026

Two-Step Tag-Free Isolation of Mitochondria for Improved Protein Discovery and Quantification
09:04

Two-Step Tag-Free Isolation of Mitochondria for Improved Protein Discovery and Quantification

Published on: June 2, 2023

The mitochondrial proteome database: MitoP2.

M Elstner1, C Andreoli, T Klopstock

  • 1Institute of Human Genetics, Helmholtz Zentrum Munich-German Research Center for Environmental Health, Neuherberg, Germany.

Methods in Enzymology
|May 12, 2009
PubMed
Summary
This summary is machine-generated.

MitoP2 consolidates mitochondrial protein data, aiding research into organelle function and disease. This database aids scientists in understanding mitochondrial proteins across species, improving research accessibility.

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Two-Step Tag-Free Isolation of Mitochondria for Improved Protein Discovery and Quantification
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Area of Science:

  • Mitochondrial biology
  • Proteomics
  • Bioinformatics

Background:

  • Mitochondrial functions, including energy production and metabolism, are critical for cellular health.
  • Understanding the mitochondrial proteome is essential for diagnosing and treating mitochondrial diseases.
  • Emerging roles in cell signaling and death highlight the need for comprehensive protein data.

Purpose of the Study:

  • To create a centralized, accessible database (MitoP2) for mitochondrial proteins.
  • To integrate data from various species for comparative proteomic analysis.
  • To provide tools for identifying and validating mitochondrial proteins.

Main Methods:

  • Consolidation of data from single protein studies and genome-wide approaches.
  • Development of a support vector machine (SVM) for predicting mitochondrial localization.
  • Manual curation of manually validated proteins for a high-confidence reference set.

Main Results:

  • MitoP2 database established with over 590 yeast, 920 human, and 1020 mouse entries.
  • SVM model provides a score for predicting mitochondrial protein localization.
  • Database offers multiple search functionalities, including disease-related proteins and mouse models.

Conclusions:

  • MitoP2 serves as a valuable resource for researchers studying mitochondrial physiology and pathology.
  • The database facilitates the interrogation of mitochondrial proteomes across different species.
  • Accessible data and predictive tools enhance the study of mitochondrial dysfunction.