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Related Concept Videos

Protein Import into the Peroxisomes01:27

Protein Import into the Peroxisomes

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Cells contain membrane-bound organelles called peroxisomes that oxidize organic molecules by transferring hydrogen atoms to oxygen, producing hydrogen peroxide. Peroxisomes enzymatically convert the released hydrogen peroxide into water and oxygen.
Peroxisomal Protein Import:
Peroxisomes lack the genetic machinery required to code for their own proteins. Hence, most peroxisomal membrane, lumenal and transmembrane proteins are synthesized in the cytoplasm or ER and transported to the peroxisome...
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Peroxisomes01:24

Peroxisomes

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Peroxisomes are specialized organelles present in fungi, plant, and animal cells. It can vary in number, size, morphology, and activity depending on the type of tissue and the nutritional state of the cell. For example, cells with active lipid metabolism, such as adipocytes, neurons, and hepatocytes, have more peroxisomes than other cells in the body. Besides their primary role in breaking down complex organic molecules, peroxisomes can also synthesize specific macromolecules and participate in...
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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.
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Protein Transport to the Thylakoids01:22

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Thylakoids are membrane-bound sac-like structures within the chloroplast that serve as sites for photosynthesis. Thylakoid lumen contains many electron transport proteins and is enclosed by a thylakoid membrane rich in the light-harvesting complex. Proteins targeted to the thylakoids are transported as precursors and are sorted by the general TOC/TIC import pathway. Once the precursor reaches the stroma, stromal processing peptidases remove their transit signal and expose thylakoid signal...
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Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

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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.
Most of the mitochondrial...
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Protein Transport to the Outer Chloroplast Membrane01:11

Protein Transport to the Outer Chloroplast Membrane

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Chloroplast outer membrane proteins encoded by the nucleus are synthesized in the cytosol. Soon after synthesis, they bind cytosolic factors such as 14-3-3 protein and the Hsp70 chaperones that keep these precursors in an unfolded state until their translocation.
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The type-2 peroxisomal targeting signal.

Markus Kunze1

  • 1Medical University of Vienna, Center for Brain Research, Department of Pathobiology of the Nervous System, Spitalgasse 4, 1090 Vienna, Austria.

Biochimica Et Biophysica Acta. Molecular Cell Research
|November 22, 2019
PubMed
Summary

The type-2 peroxisomal targeting signal (PTS2) directs proteins to peroxisomes via the PEX7 receptor. Defects in this import pathway cause severe inherited diseases like rhizomelic chondrodysplasia punctata.

Keywords:
EvolutionPTS2Peptide recognitionPeroxisomesProtein transportTargeting signals

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • Peroxisomes are vital organelles involved in various metabolic processes.
  • Protein import into peroxisomes is crucial for cellular function.
  • The type-2 peroxisomal targeting signal (PTS2) is a key motif for targeting specific proteins to peroxisomes.

Purpose of the Study:

  • To elucidate the mechanism of PTS2-mediated protein import into peroxisomes.
  • To understand the role of the PEX7 receptor and its co-receptor in PTS2 targeting.
  • To investigate the functional and structural relationship between PTS2 and other targeting signals.

Main Methods:

  • Analysis of PTS2 motif structure and conserved residues.
  • Investigation of the PEX7-co-receptor complex formation and function.
  • Study of protein translocation across the peroxisomal membrane.
  • Examination of the ubiquitin-mediated export mechanism of receptor components.

Main Results:

  • PTS2 functions as an amphipathic alpha-helix, exposing conserved residues on one side.
  • The PEX7-co-receptor complex mediates cargo recognition and translocation.
  • Protein release and receptor recycling involve a ubiquitin-mediated, ATP-dependent process.
  • Defective PTS2 import leads to severe inherited disorders, such as rhizomelic chondrodysplasia punctata.

Conclusions:

  • The PTS2 pathway is essential for peroxisomal protein import and cellular homeostasis.
  • Dysfunctional PTS2 import underlies severe human genetic diseases.
  • Further research is needed to clarify the relationship between PTS2 and PTS1 targeting mechanisms.