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Related Concept Videos

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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.
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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.
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The cell membrane, or plasma membrane, is an ever-changing landscape. It is described as a fluid mosaic where various macromolecules are embedded in the phospholipid bilayer. Among the macromolecules are proteins. The protein content varies across cell types. For example, mitochondrial inner membranes contain ~76% protein content, while myelin contains ~18% protein content. Individual cells contain many types of membrane proteins—red blood cells contain over 50—and different cell...
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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...
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Plant Mitochondrial Inner Membrane Protein Insertion.

Renuka Kolli1, Jürgen Soll2,3, Chris Carrie4

  • 1Department of Biology I, Botany, Ludwig-Maximilians-Universität München, Großhaderner Strasse 2-4, D-82152 Planegg-Martinsried, Germany. renuka.kolli@biologie.uni-muenchen.de.

International Journal of Molecular Sciences
|March 3, 2018
PubMed
Summary

Plant mitochondria utilize unique protein insertion machinery, including the Oxa and Tat pathways, differing from yeast and humans. This review explores these distinct mechanisms and their evolutionary significance.

Keywords:
Oxamembrane insertionplant mitochondriatwin-arginine translocation

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Area of Science:

  • Mitochondrial biogenesis
  • Protein targeting and insertion
  • Plant cell biology

Background:

  • Mitochondrial inner membrane proteins are crucial for cellular respiration.
  • Protein insertion into the inner mitochondrial membrane involves conserved machineries like TIM23, TIM22, and Oxa.
  • Plant mitochondria possess unique features impacting protein import.

Purpose of the Study:

  • To review the unique aspects of plant mitochondrial inner membrane protein insertion machinery.
  • To compare plant mechanisms with those in yeast and humans.
  • To highlight lineage-specific similarities and differences in protein biogenesis.

Main Methods:

  • Comparative analysis of protein insertion machineries across different species.
  • Case study on the biogenesis of cytochrome c oxidase subunit 2 (Cox2).
  • Review of existing literature on mitochondrial protein import.

Main Results:

  • Plant mitochondria employ distinct protein insertion pathways compared to other eukaryotes.
  • The Oxa machinery is conserved from bacterial ancestors for specific protein insertions.
  • Plant mitochondria may use the Tat machinery for Rieske Fe/S protein insertion, similar to bacteria and chloroplasts.

Conclusions:

  • Plant mitochondrial protein insertion exhibits unique evolutionary adaptations.
  • Understanding these differences is key to comprehending plant mitochondrial function.
  • The Tat machinery's role in plant mitochondria represents a significant divergence from other eukaryotes.