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Related Concept Videos

Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

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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...
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Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

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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...
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Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

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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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Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

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

Protein Transport into the Inner 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.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
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Structure of Porins01:21

Structure of Porins

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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...
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Assessment of Submitochondrial Protein Localization in Budding Yeast Saccharomyces cerevisiae
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The potato tuber mitochondrial proteome.

Fernanda Salvato1, Jesper F Havelund, Mingjie Chen

  • 1Department of Biochemistry and Interdisciplinary Plant Group, University of Missouri, Columbia, Missouri 65211.

Plant Physiology
|December 20, 2013
PubMed
Summary
This summary is machine-generated.

This study identified over 1,000 potato tuber mitochondrial proteins, revealing new insights into plant metabolism and mitochondrial function. The research provides a comprehensive proteome map, including many previously unconfirmed proteins.

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Area of Science:

  • Plant Biology
  • Mitochondrial Proteomics
  • Biochemistry

Background:

  • Mitochondria are vital for cellular energy production and metabolism.
  • Understanding mitochondrial roles in storage tissues like potato tubers is crucial for plant science.
  • Previous studies lacked comprehensive proteome data for plant mitochondria.

Purpose of the Study:

  • To comprehensively identify and quantify proteins in dormant potato tuber mitochondria.
  • To investigate the role of mitochondria in regulating metabolism in storage tissues.
  • To establish a high-coverage proteome map of plant mitochondria.

Main Methods:

  • Isolation of highly purified mitochondria from dormant potato tubers.
  • Proteome analysis using one-dimensional gel electrophoresis and liquid chromatography-tandem mass spectrometry (LC-MS/MS) on an Orbitrap XL.
  • Quantitative analysis of identified proteins using normalized spectral counts and four search programs.

Main Results:

  • Identification of 1,060 nonredundant potato tuber mitochondrial proteins, with high coverage (up to 85%) of the proteome.
  • Quantification revealed a dynamic range of 1,800-fold, including key metabolic pathway components.
  • Discovery of 71 pentatricopeptide repeat proteins, 29 membrane carriers, and novel proteins in coenzyme/iron metabolism; over 50% of proteins showed posttranslational modifications, predominantly oxidative.

Conclusions:

  • This study presents a near-comprehensive proteome of potato tuber mitochondria, significantly expanding the known plant mitochondrial proteome.
  • The findings offer a foundation for understanding mitochondrial regulation of metabolism in storage organs.
  • The developed strategy enables unbiased, extensive identification of mitochondrial proteins and their modifications.