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Related Concept Videos

The Proteasome01:13

The Proteasome

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Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
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The Proteasome02:18

The Proteasome

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Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
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The Proteasome02:18

The Proteasome

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The Proteasome Structure01:17

The Proteasome Structure

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The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
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Regulated Protein Degradation02:58

Regulated Protein Degradation

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It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
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Regulated Protein Degradation02:58

Regulated Protein Degradation

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Related Experiment Video

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Quantifying Subcellular Ubiquitin-proteasome Activity in the Rodent Brain
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Pup recycling regulates the proteasome.

Anushya Petchiappan1, Dipankar Chatterji1

  • 1Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India.

The FEBS Journal
|June 20, 2017
PubMed
Summary

The bacterial Pup proteasome system (PPS) controls protein degradation similarly to the eukaryotic system. This study reveals how PPS maintains pupylation levels for regulated protein breakdown.

Area of Science:

  • Bacterial protein degradation pathways
  • Molecular mechanisms of proteasomes

Background:

  • The bacterial Pup proteasome system (PPS) is analogous to the eukaryotic ubiquitin proteasome system (UPS).
  • Understanding of PPS machinery and its regulatory mechanisms remains limited.
  • Controlled protein degradation is crucial for cellular homeostasis.

Purpose of the Study:

  • To elucidate the regulatory mechanisms governing the bacterial Pup proteasome system (PPS).
  • To understand how PPS maintains steady-state levels of protein pupylation.
  • To investigate the link between pupylation levels and controlled protein degradation in bacteria.

Main Methods:

  • Combined experimental analyses with computational modeling.
  • Investigated protein pupylation dynamics within the PPS.

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  • Assessed the impact of pupylation levels on protein degradation rates.

    • Main Results:

    • Demonstrated how the PPS actively maintains steady-state protein pupylation levels.
    • Established a clear correlation between pupylation levels and the efficiency of protein degradation.
    • Provided insights into the regulatory network controlling PPS activity.

    Conclusions:

    • The bacterial PPS employs specific mechanisms to ensure consistent pupylation.
    • This regulation is essential for precise control over protein degradation in bacteria.
    • Further research into PPS can illuminate fundamental principles of proteasomal function.