temperature range mid4

Edge evidence

• warm-mesophile adaptation enables temperature range mid4 RO:0002327

  Warm-mesophile adaptation enables growth across 34–40 °C.

  • DOI:10.1146/annurev-micro-091313-103612 more unsaturated fatty acids Supports warm-mesophile homeoviscous adaptation as the range mechanism.
• temperature range mid4 is a temperature range rdfs:subClassOf

  Temperature range mid4 is a quantitative bin of the temperature-range phenotype.

  • DOI:10.1016/s0300-9629(97)00003-0 adapted to environments of high temperature Supports the 34–40 °C range as a value within the temperature-range distribution.
• FabI/FabB fatty-acid branchpoint valve enables homeoviscous adaptation RO:0002327

  The FabI/FabB branchpoint valve reallocates flux between saturated and unsaturated fatty acid synthesis, enabling homeoviscous adaptation.

  • DOI:10.1038/s41467-024-53677-5 A temperature-sensitive metabolic valve at the fatty-acid branchpoint reallocates flux between saturated and unsaturated fatty acid synthesis via FabI and FabB.
• FabA/FabI/FabB competition for C10:1 pool regulates membrane lipid composition RO:0002211

  Competition of FabA/FabI/FabB for the common C10:1 pool shifts flux between saturated and unsaturated fatty acids, changing membrane lipid composition.

  • DOI:10.1038/s41467-024-53677-5 FabA, FabI and FabB compete for a common C10:1 pool forming a metabolic valve that shifts flux between saturated and unsaturated fatty acids.
• membrane fluidity restoration enables growth after temperature shock RO:0002327

  Valve plus transcriptional feedback restores optimal membrane fluidity within a single generation, supporting growth after a temperature shock.

  • DOI:10.1038/s41467-024-53677-5 Restores optimal membrane fluidity within a single generation after a temperature shock.
• heat stress causes protein unfolding and aggregation biolink:causes

  High temperatures cause protein unfolding and aggregation.

  • DOI:10.1186/s12864-023-09266-9 High temperatures cause a suite of problems for cells, including protein unfolding and aggregation.
• protein unfolding and aggregation causes impaired mesophile growth biolink:causes

  Protein unfolding and aggregation impairs mesophile growth unless compensated.

  • DOI:10.1186/s12864-023-09266-9 General mechanistic background applicable to the warm-mesophile upper range; protein damage impairs growth unless compensated.
• heat stress causes membrane fluidity biolink:causes

  High temperatures increase membrane fluidity, requiring compensatory adaptation.

  • DOI:10.1186/s12864-023-09266-9 High temperatures cause a suite of problems for cells, including increased membrane fluidity.
• membrane fluidity requires compensatory membrane adaptation

  Temperature-driven increase in membrane fluidity requires compensatory adaptation.

  • DOI:10.1186/s12864-023-09266-9 Increased membrane fluidity at high temperature requires compensatory adaptation to maintain function.
• sigma-32 (RpoH) heat-shock regulon induces DnaK/DnaJ/GrpE and GroES/GroEL chaperone systems

  The sigma-32/RpoH regulon induces the DnaK/DnaJ/GrpE and GroES/GroEL chaperone systems.

  • DOI:10.1128/mbio.03105-23 The alternative sigma factor sigma-32 (RpoH) drives protective heat shock proteins including the DnaK/DnaJ/GrpE and GroES/GroEL chaperone systems.
• DnaK/DnaJ/GrpE and GroES/GroEL chaperone systems enables protection against heat stress RO:0002327

  The DnaK/DnaJ/GrpE and GroES/GroEL chaperone systems protect against heat stress.

  • DOI:10.1128/mbio.03105-23 Canonical heat-response: chaperone systems refold stress-damaged proteins to protect against heat stress.