thermotolerant

Edge evidence

• elevated temperature causes heat-shock response biolink:causes

  Elevated temperature triggers heat-shock chaperone induction.

  • DOI:10.1128/MMBR.65.1.1-43.2001 resistant to irreversible inactivation at high temperatures Supports protein-stability physiology as a high-temperature response.
• chaperone proteins enables limited thermostability RO:0002327

  Chaperone proteins support limited thermostability sufficient for facultative high-temperature growth.

  • DOI:10.1128/MMBR.65.1.1-43.2001 resistant to irreversible inactivation at high temperatures Supports chaperone-mediated heat-stress tolerance.
• limited thermostability enables thermotolerant RO:0002327

  Limited thermostability enables facultative growth at elevated temperatures.

  • DOI:10.1099/00207713-52-6-2203 Pseudomonas thermotolerans sp. nov., a thermotolerant species Supports the trait endpoint in a representative organism.
• RpoH (sigma-32) heat-shock sigma factor positively regulates heat-shock chaperone gene expression

  RpoH (sigma-32) drives expression of the groEL, dnaKJ, grpE, and clpB heat-shock genes.

  • DOI:10.1186/s12934-024-02602-y The expression of groEL, dnaKJ, grpE, and clpB were regulated by the sigma factor RpoH, whose deletion led to heat sensitivity.
• heat-shock chaperone gene expression enables heat-shock response RO:0002327

  Induced chaperone/disaggregase gene expression enables the protective heat-shock response.

  • DOI:10.1186/s12934-024-02602-y groEL, dnaKJ, grpE, clpB constitute the chaperone/disaggregase machinery of the heat-shock response.
• elevated temperature causes membrane protein folding and LPS biosynthesis biolink:causes

  Heat-activated RpoE induces membrane protein folding and LPS biosynthesis to preserve envelope integrity.

  • DOI:10.1007/s12275-023-00031-x Activated RpoE induces genes involved in folding of membrane proteins and biosynthesis of lipopolysaccharides under heat shock.
• RpoE envelope-stress sigma factor positively regulates membrane protein folding and LPS biosynthesis

  RpoE envelope-stress sigma factor positively regulates membrane protein folding and LPS biosynthesis.

  • DOI:10.1007/s12275-023-00031-x Activated RpoE induces heat-shock proteins, periplasmic proteases (HtrA, DegP), and genes for membrane protein folding and LPS biosynthesis.
• unsaturated fatty acid biosynthesis contributes to thermotolerant RO:0002326

  Unsaturated fatty acid biosynthesis tunes membrane fluidity, contributing to thermotolerance.

  • DOI:10.1128/spectrum.01627-23 A sharp relationship between thermotolerance and fatty-acid metabolism; saturated/unsaturated FA balance modulates heat tolerance.
• trehalose compatible-solute accumulation positively regulates limited thermostability

  Trehalose compatible-solute accumulation stabilizes proteins and membranes against heat damage.

  • DOI:10.1186/s40694-023-00168-9 Accumulation of mannitol and trehalose as the main compatible solutes is a key factor for heat resistance.