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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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Coordination of Gene Expression Processes in Bacteria01:29

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The DNA replication, transcription, and translation processes are intricately coupled in bacteria, allowing efficient gene expression and rapid protein synthesis. While this physical and functional coordination is advantageous, it introduces challenges that bacteria overcome through specific regulatory mechanisms.Coupling of Replication, Transcription, and TranslationThe coupling of replication, transcription, and translation is a hallmark of bacterial gene expression. As the replisome unwinds...
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Porin Insertion in the Outer Mitochondrial Membrane01:12

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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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The Movement of Organelles and Vesicles01:43

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In eukaryotic cells,  cytoskeletal filaments such as actin, microtubules, and intermediate filaments form a mesh-like cytoskeletal network. These filaments serve as tracks for transporting cellular cargo. Specialized motor proteins use the chemical energy stored in adenosine triphosphate (ATP) for this transport. During interphase, microtubules are polarized, with the plus-end towards the cell periphery and the minus-end towards the cell center. Two microtubule-associated motor proteins,...
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Termination of Translation01:44

Termination of Translation

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The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
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Mitochondrial Precursor Proteins01:39

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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.
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Related Experiment Video

Updated: Dec 31, 2025

Rapid Isolation of the Mitoribosome from HEK Cells
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Rescuing stalled mammalian mitoribosomes - what can we learn from bacteria?

Shreya Ahana Ayyub1, Fei Gao1, Robert N Lightowlers2

  • 1The Wellcome Centre for Mitochondrial Research, Newcastle University, The Medical School, Framlington Place, Newcastle upon Tyne, NE2 4HH, UK.

Journal of Cell Science
|January 4, 2020
PubMed
Summary

Mammalian mitochondria lack bacterial ribosome rescue systems like trans-translation. This study explores mitochondrial translation termination factors and their potential roles in rescuing stalled mitoribosomes.

Keywords:
ArfAArfBArfTC12orf65ICT1Mammalian mitochondriaMitoribosomesMtRF1Release factorStalled ribosomeTrans-translationTranslation termination

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Last Updated: Dec 31, 2025

Rapid Isolation of the Mitoribosome from HEK Cells
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Isolation of Translating Ribosomes Containing Peptidyl-tRNAs for Functional and Structural Analyses
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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Genetics

Background:

  • Canonical protein translation involves ribosome recycling after polypeptide release.
  • Ribosome stalling can occur due to various factors impeding protein synthesis.
  • Mammalian mitochondrial ribosome rescue mechanisms differ from bacterial systems.

Purpose of the Study:

  • To overview canonical translation termination in bacteria and mammalian mitochondria.
  • To compare bacterial stalled ribosome rescue systems with mitochondrial factors.
  • To suggest potential roles for mitochondrial translation release factors in mitoribosome rescue.

Main Methods:

  • Comparative analysis of bacterial and mitochondrial translation termination.
  • Review of existing literature on ribosome rescue mechanisms.
  • Homology assessment of mitochondrial factors with bacterial rescue systems.

Main Results:

  • Mammalian mitochondria lack the bacterial trans-translation system.
  • Four translation termination factors are present in mitochondria, showing homology to bacterial backup systems.
  • No definitive evidence currently shows these factors functioning in mitoribosome rescue.

Conclusions:

  • Mitochondrial ribosome rescue likely employs distinct mechanisms compared to bacteria.
  • Mitochondrial translation termination factors represent potential candidates for ribosome rescue.
  • Further research is needed to elucidate the precise roles of these factors in mammalian mitochondria.