PerR controls peroxide- and iron-responsive expression of oxidative stress defense genes in Helicobacter hepaticus

Insights

Helicobacter hepaticus uses the PerR regulator to control genes involved in oxidative stress defense, like katA and ahpC. This regulation is crucial for the bacteria

Area of Science:

  • Microbiology
  • Bacterial Pathogenesis
  • Oxidative Stress Response

Background:

  • Chronic Helicobacter hepaticus colonization causes inflammatory diseases.
  • H. hepaticus encounters oxidative stress during colonization.
  • The PerR regulator's role in oxidative stress response is unknown.

Purpose of the Study:

  • Investigate the role of H. hepaticus PerR (HH0942) in regulating oxidative stress genes.
  • Determine the impact of PerR on katA (HH0043) and ahpC (HH1564) gene expression.
  • Understand the connection between iron metabolism and oxidative stress defense in H. hepaticus.

Main Methods:

  • Gene expression analysis (transcription and protein levels).
  • Hydrogen peroxide and iron restriction induction assays.
  • Gene inactivation studies (perR and katA mutants).

Main Results:

  • PerR regulates katA and ahpC expression, which are induced by hydrogen peroxide and iron restriction.
  • PerR inactivation leads to constitutive, iron-independent expression of katA and ahpC.
  • katA inactivation increases H. hepaticus sensitivity to hydrogen peroxide and reduces aerotolerance.

Conclusions:

  • The PerR regulatory protein connects iron metabolism and oxidative stress defense in H. hepaticus.
  • This regulatory mechanism is similar to Campylobacter jejuni but differs from Helicobacter pylori.
  • PerR-mediated regulation is essential for H. hepaticus survival under oxidative stress conditions.

Related Concept Videos

Peroxisomes01:24

Peroxisomes

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...
13.6K
Peroxisomes01:24

Peroxisomes

1.8K
Protein Import into the Peroxisomes01:27

Protein Import into the Peroxisomes

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...
4.4K
Other Stress Responses in Bacteria01:30

Other Stress Responses in Bacteria

Bacteria have global regulatory systems that control several types of stress mechanisms. These include Pho regulon and the heat shock response, which are essential systems for environmental adaptation, such as nutrient limitation and proteotoxic stress. The Pho regulon and the heat shock response exemplify bacterial resilience, enabling rapid adaptation to fluctuating environmental conditions.Pho RegulonBacteria require phosphorus for essential cellular processes, including nucleic acid...
587
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
2.2K
The Unfolded Protein Response01:37

The Unfolded Protein Response

The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
5.6K