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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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Mitochondrial Protein Sorting01:39

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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.
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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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Mitochondria01:37

Mitochondria

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Mitochondria are eukaryotic cellular organelles that are known to produce energy through a process called oxidative phosphorylation. Besides their primary function, mitochondria are involved in various cellular processes, including cell growth, differentiation, signaling, metabolism, and senescence. Age-related changes cause a decline in mitochondrial quality and integrity due to increased mitochondrial mutations and oxidative damage. Thus, aging can severely impact mitochondrial functions,...
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Animal Mitochondrial Genetics02:59

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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...
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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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Assessment of Submitochondrial Protein Localization in Budding Yeast Saccharomyces cerevisiae
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Polycomb Repressive Complex 1 and USP16 localize to the mitochondrion and influence its function.

Lei Shi1,2,3, Chunxu Chen1,2, Xiaokun Jian1,2

  • 1Department of Internal Medicine, Division of Hematology, Oncology and Palliative Care, Virginia Commonwealth University, Richmond, VA 23298.

Proceedings of the National Academy of Sciences of the United States of America
|October 14, 2025
PubMed
Summary
This summary is machine-generated.

Polycomb Repressive Complex 1 (PRC1) and USP16 are found in mitochondria, impacting mitochondrial function. Their disruption impairs mitochondrial integrity and respiratory function, revealing novel roles beyond nuclear gene regulation.

Keywords:
PRC1USP16mitochondriarespiratory functionubiquitin

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Mitochondrial Biology

Background:

  • Polycomb Repressive Complex 1 (PRC1) is known to regulate gene expression through histone modification.
  • USP16 counteracts PRC1-mediated histone H2A ubiquitination (H2Aub).
  • The non-canonical functions of nuclear proteins in mitochondria are an emerging area of research.

Purpose of the Study:

  • To investigate the localization and function of PRC1 and USP16 in mitochondria.
  • To determine the impact of PRC1 and USP16 on mitochondrial integrity and function.
  • To explore the role of the ubiquitin pathway within mitochondria concerning these proteins.

Main Methods:

  • Immunofluorescence and proximity ligation assays.
  • Cell fractionation and biochemical analyses of isolated mitochondria.
  • Mitochondria-specific depletion and gene knockout strategies (e.g., RING1/RING2 KO).

Main Results:

  • PRC1 and USP16 were found to localize within mitochondria.
  • Mitochondria-specific depletion of PRC1 subunit RING2 altered mitochondrial protein ubiquitination.
  • Disruption of PRC1 led to significant changes in mitochondrial proteome, integrity, and respiratory function.

Conclusions:

  • PRC1 and USP16 translocate to mitochondria, directly influencing mitochondrial integrity and function.
  • These proteins play a role in the mitochondrial ubiquitin pathway.
  • The study reveals novel mitochondrial roles for PRC1 and USP16 beyond their established nuclear functions.