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Related Concept Videos

The Proteasome Structure01:17

The Proteasome Structure

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...
The Proteasome02:18

The Proteasome

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.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
The Proteasome01:13

The Proteasome

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 (ubiquitin...
The Proteasome02:18

The Proteasome

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.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

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Related Experiment Video

Updated: Jul 6, 2026

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
09:57

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach

Published on: December 17, 2016

Rethinking proteasome evolution: two novel bacterial proteasomes.

Ruben E Valas1, Philip E Bourne

  • 1Bioinformatics Program, University of California, San Diego, La Jolla, CA 92093, USA. rvalas@ucsd.edu

Journal of Molecular Evolution
|April 5, 2008
PubMed
Summary

Researchers discovered two novel bacterial proteasome groups, Anbu and beta-proteobacteria proteasome homologue (BPH). These ancient structures suggest a new evolutionary path for protein degradation systems.

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Assaying Proteasomal Degradation in a Cell-free System in Plants
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Assaying Proteasomal Degradation in a Cell-free System in Plants

Published on: March 26, 2014

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Last Updated: Jul 6, 2026

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
09:57

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach

Published on: December 17, 2016

Assaying Proteasomal Degradation in a Cell-free System in Plants
07:43

Assaying Proteasomal Degradation in a Cell-free System in Plants

Published on: March 26, 2014

Area of Science:

  • Microbiology
  • Molecular Biology
  • Evolutionary Biology

Background:

  • The proteasome is a crucial cellular machine for protein degradation, essential for regulating protein homeostasis.
  • Bacterial proteasomes, like HslV, exhibit varying complexity, from single-gene to multi-gene encoded structures.
  • Eukaryotic 20S proteasomes are highly complex, encoded by over 14 genes, yet share homologous subunits with bacterial counterparts.

Purpose of the Study:

  • To investigate the diversity and evolutionary history of proteasome structures in bacteria.
  • To identify novel proteasome groups beyond known bacterial forms.
  • To explore the potential origins and functional implications of newly discovered proteasomes.

Main Methods:

  • Genome-wide search across 238 complete bacterial genomes for proteasome-related structures.
  • Sequence and structural analyses to compare novel findings with known proteasomes.
  • Phylogenetic distribution analysis to infer evolutionary relationships and age.

Main Results:

  • Identification of two novel bacterial proteasome groups: Anbu and beta-proteobacteria proteasome homologue (BPH).
  • Anbu is ancient, found in cyanobacteria and proteobacteria, potentially predating other bacterial proteasomes.
  • Anbu and BPH possess distinct homologous structures, differing from known bacterial proteasomes; Anbu's function may relate to transglutaminase activity.

Conclusions:

  • The discovery of Anbu and BPH expands the known diversity of bacterial proteasomes.
  • Anbu's ancient origin and potential role in generating more complex proteasomes, like the eukaryotic 20S proteasome, are hypothesized.
  • The presence of varied combinations of Anbu, BPH, and HslV suggests specialized protein degradation pathways in bacteria.