Related Experiment Video

Updated: Jul 2, 2026

Growth-based Determination and Biochemical Confirmation of Genetic Requirements for Protein Degradation in Saccharomyces cerevisiae
10:57

Growth-based Determination and Biochemical Confirmation of Genetic Requirements for Protein Degradation in Saccharomyces cerevisiae

Published on: February 16, 2015

Proteins involved in microbody biogenesis and degradation in Aspergillus nidulans

Jan A K W Kiel1, Ida J van der Klei

  • 1Molecular Cell Biology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, PO Box 14, NL-9750 AA Haren, The Netherlands. J.A.K.W.Kiel@RUG.nl

Fungal Genetics and Biology : FG & B
|August 13, 2008
PubMed

Insights

This study identifies conserved genes for fungal peroxisome (microbody) formation and degradation in Aspergillus nidulans. These fungi offer a model for understanding peroxisome homeostasis in humans.

Area of Science:

  • Cell Biology
  • Mycology
  • Genetics

Background:

  • Fungal microbodies, or peroxisomes, are inducible organelles crucial for cellular processes.
  • Peroxisome biogenesis involves peroxins (PEX genes), and their degradation occurs via pexophagy, utilizing autophagy-related (ATG) genes.

Purpose of the Study:

  • To re-analyze the Aspergillus nidulans genome for PEX and ATG genes.
  • To accurately determine intron positions for identified genes.
  • To compare fungal peroxisome biogenesis and degradation pathways with those in yeast and mammals.

Main Methods:

  • Genomic re-analysis of Aspergillus nidulans.
  • Manual determination of intron positions in PEX and ATG genes.
  • Comparative analysis of fungal, yeast, and mammalian peroxisome-related genes.

Main Results:

  • Identification of previously missed PEX and ATG genes in A. nidulans.
  • Confirmation of conserved core genes for peroxisome biogenesis and pexophagy in filamentous fungi.
  • Demonstration that fungal peroxisome dynamics share features with mammalian pathways, distinct from yeast.

Conclusions:

  • The fundamental genetic machinery for peroxisome homeostasis is conserved in filamentous fungi.
  • Filamentous fungi, like A. nidulans, serve as valuable models for studying human peroxisome biology.
  • Understanding fungal peroxisome dynamics provides insights into mammalian organelle homeostasis.

More Related Videos

Cycloheximide Chase Analysis of Protein Degradation in Saccharomyces cerevisiae09:05

Cycloheximide Chase Analysis of Protein Degradation in Saccharomyces cerevisiae

Published on: April 18, 2016

Reporter-based Growth Assay for Systematic Analysis of Protein Degradation07:47

Reporter-based Growth Assay for Systematic Analysis of Protein Degradation

Published on: November 6, 2014

Related Concept Videos

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...
Regulated Protein Degradation02:58

Regulated Protein Degradation

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.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Regulated Protein Degradation02:58

Regulated Protein Degradation

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.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...