temperature optimum mid4

Edge evidence

• warm host-associated environment engages warm-mesophile adaptation

  Warm host-associated environments engage warm-mesophile adaptation.

  • DOI:10.1146/annurev-micro-091313-103612 more unsaturated fatty acids Supports homoviscous adaptation at warm-mesophilic temperatures.
• warm-mesophile adaptation produces temperature optimum mid4 METPO:2000202

  Warm-mesophile adaptation yields a 34–40 °C optimum.

  • DOI:10.1146/annurev-micro-091313-103612 more unsaturated fatty acids Supports the 34–40 °C optimum as the warm-mesophile outcome.
• temperature optimum mid4 is a temperature optimum rdfs:subClassOf

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

  • DOI:10.1016/s0300-9629(97)00003-0 adapted to environments of high temperature Supports the 34–40 °C optimum as a value within the temperature-optimum distribution.
• temperature downshift increases unsaturated fatty acid proportion RO:0002213

  Temperature downshift increases the proportion of unsaturated fatty acids (homeoviscous adaptation).

  • DOI:10.1146/annurev-micro-091313-103612 Bacteria perform homeoviscous adaptation by incorporating proportionally more unsaturated fatty acids as growth temperature decreases.
• unsaturated fatty acid proportion maintains membrane fluidity homeostasis

  Increased unsaturated fatty acids maintain membrane fluidity homeostasis.

  • DOI:10.1146/annurev-micro-091313-103612 Disrupting bilayer order optimizes cellular processes at the new temperature; membrane fluidity homeostasis.
• membrane fluidity homeostasis induces unsaturated fatty acid biosynthesis response

  Sensed decreases in membrane fluidity induce the unsaturated fatty acid biosynthesis response.

  • DOI:10.1146/annurev-micro-091313-103612 Microbes sense decreases in membrane fluidity and initiate responses that upregulate biosynthesis of unsaturated fatty acids.
• RNA thermometer hairpin occludes Shine-Dalgarno / AUG ribosome binding site

  RNA thermometer hairpins occlude the Shine-Dalgarno/AUG region, repressing translation at low temperature.

  • DOI:10.1007/s12275-023-00031-x ROSE and FourU RNA thermometers form inhibitory hairpins that cover Shine-Dalgarno/AUG.
• temperature upshift / heat shock melts RNA thermometer hairpin

  Temperature upshift / heat shock melts RNA thermometer structures.

  • DOI:10.1007/s12275-023-00031-x RNA thermometers are stable at low temperatures but undergo conformational change (melting) at heat shock.
• RNA thermometer hairpin enables ribosome binding and translation initiation RO:0002327

  Melting of the RNA thermometer exposes the ribosome binding site and enables translation initiation.

  • DOI:10.1007/s12275-023-00031-x Melting releases translation inhibition, allowing ribosome binding and translation initiation.
• DnaK chaperone negatively regulates RpoH (sigma-32) heat-shock sigma factor

  DnaK binds and retains RpoH, negatively regulating the heat-shock sigma factor.

  • DOI:10.1007/s12275-023-00031-x DnaK binds and retains RpoH until heat-denatured proteins displace it.
• FtsH protease controls abundance of RpoH (sigma-32) heat-shock sigma factor

  FtsH protease controls RpoH protein levels.

  • DOI:10.1007/s12275-023-00031-x ATP-dependent proteases FtsH and ClpXP control RpoH protein levels.