6.20

Other Stress Responses in Bacteria

648 views01:30 min

Bacteria manage stress through regulatory systems, such as the Pho regulon, which helps respond to phosphorus scarcity.

This system uses a two-component signal transduction consisting of PhoR, a sensor, and PhoB, a response regulator.

During phosphorus scarcity, PhoR detects low phosphorus, autophosphorylates, and transfers the phosphate to PhoB, activating phosphorus uptake genes.

Conversely, when phosphorus is abundant, PhoB dephosphorylates, downregulating these genes.

Bacteria also face stress due to protein damage from heat, chemicals, and radiation.

σ³², also called RpoH, is involved in activating the expression of heat shock proteins.

Under non-stress conditions, the chaperone protein DnaK binds to σ³², preventing an excessive heat shock response.

During stress, DnaK preferentially binds misfolded proteins, freeing σ³² to increase heat shock protein expression.

Once the stress subsides and proteins are properly refolded, DnaK resumes binding to σ³², reducing heat shock protein levels.

Additionally, certain proteases are induced as part of the heat shock response and degrade denatured or aggregated proteins.

Overview

Loading...

$$\rightleftharpoonup{xx}$$ $$\longleftharp{xx}$$, $$\longrightharp{xx}$$,

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 Regulon

Bacteria require phosphorus for essential cellular processes, including nucleic acid synthesis, energy metabolism, and membrane integrity. The Pho regulon is a global regulatory network that enables bacteria to adapt to phosphorus scarcity through a two-component system consisting of the sensor kinase PhoR and the response regulator PhoB. Under low-phosphorus conditions, PhoR undergoes autophosphorylation and transfers the phosphate group to PhoB, activating it. Phosphorylated PhoB then upregulates phosphate uptake and metabolism genes, including phoA, pstS, and ugpB, facilitating increased phosphorus acquisition. Conversely, when phosphorus is abundant, PhoB is dephosphorylated, leading to the downregulation of these genes, thereby conserving energy and preventing excessive phosphate accumulation.

Heat Shock Response

Apart from nutrient scarcity, bacterial cells are also frequently exposed to proteotoxic stress, including elevated temperatures, oxidative stress, and chemical denaturants, all of which can cause protein misfolding and aggregation. The heat shock response is mediated by the alternative sigma factor σ³² (RpoH), which regulates the expression of heat shock proteins (HSPs). Under normal conditions, σ³² is bound and sequestered by the molecular chaperone DnaK, keeping the heat shock response in check. However, when misfolded proteins accumulate due to stress, DnaK preferentially binds these aberrant proteins, liberating σ³². This leads to increased transcription of heat shock genes encoding chaperones such as DnaK, GroEL, and GroES, which aid in protein refolding. Additionally, ATP-dependent proteases degrade irreversibly damaged proteins, preventing toxic aggregation. Once the stress subsides, properly refolded proteins release DnaK, which rebinds σ³², restoring the system to its basal state.

Transcript

Explore More Videos

Heat Shock Response

Phosphorus Scarcity

Proteotoxic Stress

Two Component System

Sigma Factor 32

Phosphate Uptake

Heat Shock Proteins

Molecular Chaperone DnaK

ATP Dependent Proteases