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Related Concept Videos

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...
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...
Protein Transport into the Inner Mitochondrial Membrane01:34

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...
Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
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...
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,...

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Related Experiment Video

Updated: Jul 18, 2026

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve
09:13

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve

Published on: June 14, 2017

Mitoproteome: human heart mitochondrial protein sequence database.

Purnima Guda1, Shankar Subramaniam, Chittibabu Guda

  • 1Gen*NY*sis Center for Excellence in Cancer Genomics, State University of New York at Albany, Rensselaer, NY, USA.

Methods in Molecular Biology (Clifton, N.J.)
|December 19, 2006
PubMed
Summary

A comprehensive human mitochondrial proteome database was created using experimental data and computational predictions. This resource integrates diverse information on mitochondrial proteins, aiding research in human health and disease.

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An Integrated Approach for Microprotein Identification and Sequence Analysis
09:37

An Integrated Approach for Microprotein Identification and Sequence Analysis

Published on: July 12, 2022

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Last Updated: Jul 18, 2026

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve
09:13

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve

Published on: June 14, 2017

An Integrated Approach for Microprotein Identification and Sequence Analysis
09:37

An Integrated Approach for Microprotein Identification and Sequence Analysis

Published on: July 12, 2022

Area of Science:

  • Mitochondrial biology
  • Proteomics
  • Bioinformatics

Background:

  • Mitochondria play crucial roles in cellular energy production and are implicated in numerous diseases.
  • Understanding the human mitochondrial proteome is essential for deciphering cellular functions and disease mechanisms.
  • Existing data on mitochondrial proteins are fragmented across various repositories.

Purpose of the Study:

  • To develop a centralized and curated human mitochondrial proteome database.
  • To integrate experimental and computational data for a comprehensive protein inventory.
  • To provide detailed annotations for mitochondrial proteins, including function, structure, and disease associations.

Main Methods:

  • Data acquisition from public repositories and experimental studies using highly purified human heart mitochondria.
  • Computational predictions using MITOPRED, a genome-scale method for identifying nucleus-encoded mitochondrial proteins.
  • Clustering of protein sequences to create a nonredundant dataset and annotation using UNIX and Perl scripts from public databases.

Main Results:

  • A nonredundant dataset of human mitochondrial proteins was generated.
  • Comprehensive annotations covering protein function, structure, disease association, and pathways were collected.
  • The database integrates diverse data sources, providing a unified view of the mitochondrial proteome.

Conclusions:

  • The developed human mitochondrial proteome database serves as a valuable resource for researchers.
  • It facilitates deeper investigation into mitochondrial functions, cellular processes, and disease pathogenesis.
  • The integrated approach ensures data accuracy and completeness for enhanced scientific discovery.