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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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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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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 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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Energy to Drive Translocation01:37

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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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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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eIF5A coordinates the transcription and translation of its target genes.

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Related Experiment Video

Updated: Oct 3, 2025

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
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Role of eIF5A in Mitochondrial Function.

Marina Barba-Aliaga1,2, Paula Alepuz1,2

  • 1Instituto de Biotecnología y Biomedicina (Biotecmed), Universitat de València, 46100 València, Spain.

International Journal of Molecular Sciences
|February 15, 2022
PubMed
Summary
This summary is machine-generated.

The eukaryotic translation initiation factor 5A (eIF5A) protein is crucial for cellular processes and linked to aging and disease. This review explores its role in maintaining healthy mitochondria and energy metabolism.

Keywords:
OXPHOSTCAeIF5Amitochondriamitochondrial respirationspermidinetranslation

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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • The eukaryotic translation initiation factor 5A (eIF5A) is essential for protein synthesis, particularly for translating specific peptide motifs.
  • eIF5A is implicated in diverse cellular functions including mRNA export, decay, proliferation, and apoptosis.
  • Declining eIF5A levels are associated with aging, while elevated levels show rejuvenating effects.

Purpose of the Study:

  • To review the current understanding of the link between eIF5A and mitochondrial function.
  • To explore the potential role of eIF5A in regulating mitochondrial homeostasis.
  • To highlight eIF5A as a potential therapeutic target for metabolic diseases.

Main Methods:

  • Literature review of studies investigating eIF5A's molecular functions.
  • Analysis of data linking eIF5A to mitochondrial respiration and metabolism.
  • Discussion of experimental evidence on eIF5A's impact on mitochondrial dynamics and enzyme levels.

Main Results:

  • eIF5A is upregulated during respiratory metabolism and its deficiency impairs mitochondrial function.
  • eIF5A deficiency leads to reduced oxygen consumption, ATP production, and altered mitochondrial dynamics.
  • Accumulating evidence strongly suggests a role for eIF5A in maintaining mitochondrial health.

Conclusions:

  • The precise molecular mechanisms of eIF5A's mitochondrial regulation remain to be elucidated.
  • eIF5A plays a significant role in mitochondrial homeostasis and energy metabolism.
  • Targeting eIF5A may offer therapeutic strategies for diseases associated with mitochondrial dysfunction and metabolic disorders.