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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...
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...
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,...
Energy to Drive Translocation01:37

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...
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...
Structure of Porins01:21

Structure of Porins

Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel precursors...

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Analyzing Mitochondrial Morphology Through Simulation Supervised Learning
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Analyzing Mitochondrial Morphology Through Simulation Supervised Learning

Published on: March 3, 2023

Modeling mitochondrial protein evolution using structural information.

Pietro Liò1, Nick Goldman

  • 1Department of Zoology, University of Cambridge, Downing Street, Cambridge CB2 3EJ, UK.

Journal of Molecular Evolution
|April 17, 2002
PubMed
Summary
This summary is machine-generated.

New protein evolution models incorporating structural data improve phylogenetic analyses, especially for distantly related species. These models offer better insights into mitochondrial protein evolution across diverse organisms.

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Area of Science:

  • Evolutionary biology
  • Molecular evolution
  • Bioinformatics

Background:

  • Phylogenetic analyses rely on models of sequence evolution.
  • Existing models may not fully capture evolutionary dynamics of mitochondrial proteins.
  • Structural properties can influence protein evolution.

Purpose of the Study:

  • To develop and evaluate new models of protein sequence evolution.
  • To incorporate structural properties of mitochondrial proteins into evolutionary models.
  • To compare the performance of new models against existing ones.

Main Methods:

  • Developed novel models of protein sequence evolution.
  • Incorporated secondary structure information from mitochondrial proteins.
  • Tested models on mitochondrial protein datasets from various taxa.

Main Results:

  • New models are comparable to existing ones for closely related mammals.
  • New models significantly improve evolutionary descriptions for diverse organisms (fungi, plants, bacteria).
  • Models incorporating structural data enhance phylogenetic accuracy for distantly related species.

Conclusions:

  • Models based on mitochondrial protein structure offer improved phylogenetic estimations.
  • These models are particularly valuable for studying evolution across broad taxonomic ranges.
  • The findings aid in understanding mitochondrial protein evolution and constructing accurate phylogenies.