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Related Concept Videos

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.
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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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The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
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ATP Synthase: Mechanism01:48

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In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
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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.
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Pharmacogenetics of Phase II Enzymes: N-acetyltransferase, Thiopurine S-methyltransferase, UDP-glucuronosyltransferase01:27

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Phase II biotransformation reactions are essential for detoxifying and eliminating xenobiotics, including many pharmaceutical compounds. These reactions typically involve conjugation, the covalent attachment of polar endogenous groups such as glucuronic acid, sulfate, methyl, or acetyl moieties to functional groups introduced during Phase I metabolism. The resulting conjugates are more water-soluble, enabling efficient renal or biliary excretion.The major classes of Phase II enzymes include...
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Tissue transglutaminase (TG2) and mitochondrial function and dysfunction.

Thung-S Lai1, Cheng-Jui Lin2, Yu-Ting Wu3

  • 1Institute of Biomedical Science, Mackay Medical College, New Taipei City, Taiwan, ROC, lai00002@mmc.edu.tw.

Frontiers in Bioscience (Landmark Edition)
|February 16, 2017
PubMed
Summary
This summary is machine-generated.

Dysfunctional mitochondria and oxidative stress activate tissue transglutaminase (TG2). This enzyme impacts mitochondrial function, gene transcription, and protein aggregation, contributing to diseases like neurodegeneration.

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Mitochondrial Biology

Background:

  • Mitochondria are vital for cellular energy production.
  • Mitochondrial dysfunction leads to oxidative stress and calcium imbalance, characteristic of mitochondrial diseases.
  • Oxidative stress can activate enzymes like tissue transglutaminase (TG2).

Purpose of the Study:

  • To explore the role of tissue transglutaminase (TG2) in mitochondrial dysfunction and disease.
  • To understand how TG2-mediated post-translational modifications (PTMs) impact mitochondrial function.
  • To summarize the interplay between dysfunctional mitochondria and TG2 activity in neurodegenerative disorders.

Main Methods:

  • Review of existing literature on mitochondrial dysfunction, oxidative stress, and TG2.
  • Analysis of TG2's role as a post-translational modification enzyme.
  • Examination of TG2's impact on gene transcription (e.g., PGC-1alpha, cytochrome C) and protein aggregation.

Main Results:

  • TG2 is induced by oxidative stress and activated by calcium elevations.
  • TG2 modulates the assembly of respiratory chain complexes and the transcription of key mitochondrial genes.
  • TG2 activity influences critical protein aggregation and metabolic enzyme function.
  • Dysfunctional mitochondria, particularly in neurodegenerative diseases, can alter TG2 activity.

Conclusions:

  • TG2 plays a significant role in both normal mitochondrial function and the pathophysiology of mitochondrial diseases.
  • Understanding TG2's function is crucial for developing therapeutic strategies for mitochondrial disorders.
  • TG2-mediated PTMs represent an emerging area of research with implications for cellular health and disease.