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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...
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

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The Inner Mitochondrial Membrane01:28

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...

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Intrinsically disordered proteins in human mitochondria.

Masahiro Ito1, Yukako Tohsato, Hitoshi Sugisawa

  • 1Department of Bioinformatics, College of Life Sciences, Ritsumeikan University, Kusatsu, Shiga 525-8577, Japan.

Genes to Cells : Devoted to Molecular & Cellular Mechanisms
|August 23, 2012
PubMed
Summary

Intrinsically disordered proteins (IDPs) are less common in mitochondria than in eukaryotes, with bacterial-like proteins showing lower disorder than host-derived ones. This suggests evolutionary origin, not location, influences IDP prevalence in mitochondria.

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Area of Science:

  • Mitochondrial Biology
  • Protein Science
  • Evolutionary Biology

Background:

  • Intrinsically disordered proteins (IDPs) are prevalent in eukaryotes but rare in prokaryotes.
  • Mitochondria, originating from α-proteobacteria, represent an evolutionary link between prokaryotes and eukaryotes.
  • The abundance of IDPs within mitochondria requires clarification due to their unique evolutionary position.

Purpose of the Study:

  • To investigate the prevalence and characteristics of intrinsically disordered proteins (IDPs) in human mitochondria.
  • To determine if the evolutionary origin of mitochondrial proteins influences their intrinsic disorder content.
  • To compare IDP levels in mitochondrially-encoded proteins versus host-encoded proteins within mitochondria.

Main Methods:

  • Retrieved 706 human mitochondrial proteins from UniProt.
  • Extracted intrinsically disordered region information using the DICHOT database.
  • Performed BLAST searches against α-proteobacterial proteins to classify mitochondrial proteins into bacterial-descended (B-type) and host-derived (E-type).

Main Results:

  • Identified 387 B-type and 319 E-type mitochondrial proteins.
  • Observed significantly lower average ID ratios in B-type proteins (10.3%) compared to E-type proteins (21.4%).
  • Found no strong correlation between mitochondrial subcompartment and IDP ratios, suggesting evolutionary origin is a key factor.

Conclusions:

  • The evolutionary origin of mitochondrial proteins significantly impacts their intrinsic disorder content.
  • Bacterial-derived mitochondrial proteins exhibit less intrinsic disorder than those acquired later from the host.
  • Intrinsic disorder prevalence in mitochondria is primarily shaped by evolutionary history rather than functional localization.