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Related Concept Videos

Translation01:31

Translation

Lesson: Translation
Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes the final step in the expression of genes. This process is carried out by ribosomes, complexes of protein and specialized RNA molecules. Ribosomes, transfer RNA (tRNA), and other proteins produce a chain of amino acids—the polypeptide—as the end product of translation.
Translation Produces the Building Blocks of Life
Translation01:31

Translation

Lesson: Translation
Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes the final step in the expression of genes. This process is carried out by ribosomes, complexes of protein and specialized RNA molecules. Ribosomes, transfer RNA (tRNA), and other proteins produce a chain of amino acids—the polypeptide—as the end product of translation.
Translation Produces the Building Blocks of Life
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

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 ATP...
Electron Transport Chain: Complex I and II01:46

Electron Transport Chain: Complex I and II

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.
ROS generation is regulated and maintained at moderate levels necessary...
Animal Mitochondrial Genetics02:59

Animal Mitochondrial Genetics

Among all the organelles in an animal cell, only mitochondria have their own independent genomes. Animal mitochondrial DNA is a double-stranded, closed-circular molecule with around 20,000 base pairs. Mitochondrial DNA is unique in that one of its two strands, the heavy, or H, -strand is guanine rich, whereas the complementary strand is cytosine rich and called the light, or L, -strand. Compared to nuclear DNA, mitochondrial DNA has a very low percentage of non-coding regions and is marked by...
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,...

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Related Experiment Video

Updated: May 11, 2026

Visualization of Mitochondrial Respiratory Function using Cytochrome C Oxidase / Succinate Dehydrogenase (COX/SDH) Double-labeling Histochemistry
06:53

Visualization of Mitochondrial Respiratory Function using Cytochrome C Oxidase / Succinate Dehydrogenase (COX/SDH) Double-labeling Histochemistry

Published on: November 23, 2011

Multilevel functional and structural defects induced by two pathogenic mitochondrial tRNA mutations.

Meng Wang1, Xiao-Long Zhou, Ru-Juan Liu

  • 1Center for RNA Research, State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, The Chinese Academy of Sciences, Shanghai 200031, People's Republic of China.

The Biochemical Journal
|May 2, 2013
PubMed
Summary
This summary is machine-generated.

Point mutations in human mitochondrial tRNAs (hmtRNAs) cause disease. Two specific hmtRNA mutations disrupt tRNA structure and function, impacting mitochondrial protein synthesis and potentially leading to disease.

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Last Updated: May 11, 2026

Visualization of Mitochondrial Respiratory Function using Cytochrome C Oxidase / Succinate Dehydrogenase (COX/SDH) Double-labeling Histochemistry
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Published on: November 23, 2011

Using Live Cell STED Imaging to Visualize Mitochondrial Inner Membrane Ultrastructure in Neuronal Cell Models
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Using Live Cell STED Imaging to Visualize Mitochondrial Inner Membrane Ultrastructure in Neuronal Cell Models

Published on: June 30, 2023

Area of Science:

  • Mitochondrial biology
  • Molecular genetics
  • Biochemistry

Background:

  • Point mutations in human mitochondrial tRNAs (hmtRNAs) are linked to disorders like chronic progressive external ophthalmoplegia (CPEO) and mitochondrial myopathy (MM).
  • Mitochondrial tRNALeu, particularly the UUR isoacceptor, is a common site for pathogenic mutations.
  • Forty mutations have been identified in hmtRNAsLeu.

Purpose of the Study:

  • To investigate the functional consequences of two specific substitutions in the TΨC arms of hmtRNAsLeu isoacceptors.
  • To elucidate the impact of these mutations on tRNA structure, processing, and protein synthesis.

Main Methods:

  • RNase probing to assess structural changes in tRNA.
  • Measurement of aminoacylation efficiency.
  • Analysis of 3'-end processing and base modification.
  • Assessment of binding to human mitochondrial elongation factor Tu (hmEF-Tu).

Main Results:

  • The G52A substitution (G12315A in tRNALeu(CUN), G3283A in tRNALeu(UUR)) caused structural alterations in the tRNA TΨC arm, reduced aminoacylation, 3'-end processing, and base modification.
  • The A57G substitution (A12320G in tRNALeu(CUN), A3288G in tRNALeu(UUR)) primarily affected aminoacylation activity and binding to hmEF-Tu.
  • These mutations collectively suggest a broad impact on mitochondrial protein synthesis.

Conclusions:

  • Specific hmtRNA mutations can induce significant structural and functional defects.
  • These defects impair key steps in mitochondrial protein synthesis, potentially amplifying disease severity.
  • Understanding tRNA dysfunction is crucial for developing therapies for mitochondrial diseases.