temperature optimum low

Edge evidence

• cool environment engages psychrotolerant adaptation

  Cool environments engage psychrotolerant adaptation programs.

  • DOI:10.1038/sj.embor.7400662 decreased membrane fluidity Supports cool-temperature membrane-stress responses as the basis of cool-range optima.
• psychrotolerant adaptation produces temperature optimum low METPO:2000202

  Psychrotolerant adaptation yields a 10–22 °C temperature optimum.

  • DOI:10.1146/annurev-micro-091313-103612 more unsaturated fatty acids Supports homoviscous adaptation as the mechanism setting cool-range optima.
• temperature optimum low is a temperature optimum rdfs:subClassOf

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

  • DOI:10.1038/sj.embor.7400662 growing well at temperatures around the freezing point of water Supports a 10–22 °C optimum as a value within the temperature-optimum distribution.
• fatty-acyl unsaturation increases membrane fluidity RO:0002213

  Increased fatty-acyl unsaturation fluidizes the membrane.

  • DOI:10.1128/spectrum.03925-23 fluidizing the membrane and reducing bilayer thickness; broadly generalizable homeoviscous adaptation.
• low temperature induces cold shock proteins

  Low temperature induces cold shock proteins.

  • DOI:10.37256/amtt.5220244537 CSPs induced at high levels during temperature shifts below 20 C.
• low temperature promotes accumulation of compatible solutes

  Low temperature promotes accumulation of compatible solutes.

  • DOI:10.37256/amtt.5220244537 Compatible solutes listed: glycine, betaine, glycerol, trehalose, sucrose, mannitol, sorbitol.
• compatible solutes stabilizes protein and membrane stabilization

  Compatible solutes stabilize proteins and membranes and depress freezing point.

  • DOI:10.37256/amtt.5220244537 with functions in freezing-point depression and stabilization.
• ice-binding/antifreeze proteins inhibits ice crystal growth RO:0002212

  Ice-binding/antifreeze proteins bind ice surfaces and inhibit ice growth/recrystallization.

  • DOI:10.37256/amtt.5220244537 AFGPs play crucial roles in protecting cells by binding to ice crystal surfaces.
• low temperature increases oxidative stress RO:0002213

  Low temperature increases oxygen solubility and ROS/oxidative stress.

  • DOI:10.37256/amtt.5220244537 Cold causes increased oxygen solubility and ROS.
• PUFA biosynthesis maintains membrane fluidity

  PUFA biosynthesis maintains membrane fluidity at low temperature.

  • DOI:10.3390/genes14010158 maintain membrane fluidity; broadly generalizable mechanism.