temperature range very low

Edge evidence

• psychrophile cold-adapted machinery enables temperature range very low RO:0002327

  Psychrophile cold-adapted machinery enables growth at ≤ 10 °C.

  • DOI:10.1038/sj.embor.7400662 decreased membrane fluidity Supports cold-adapted membranes and enzymes as enablers of growth at very low temperatures.
• temperature range very low is a temperature range rdfs:subClassOf

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

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

  Homeoviscous adaptation via lipid desaturation maintains membrane fluidity in the cold.

  • DOI:10.1007/s42770-023-01057-4 Cells adapt membrane composition (increasing double bonds in lipids) to maintain fluidity and function.
• low temperature activates two-component cold signaling RO:0002213

  Cold-induced membrane state changes activate two-component cold signaling.

  • DOI:10.1007/s42770-023-01057-4 Cold sensing occurs via changes in the liquid-crystalline state of membranes that activate two-component signaling systems.
• cold-shock proteins (CspA-family) acts on mRNA/RNA secondary structure

  CspA-family RNA chaperones resolve cold-stabilized RNA structures to sustain translation.

  • DOI:10.1007/s42770-023-01057-4 Cold-shock proteins (CSPs) act on mRNAs; increased levels of nucleic-acid-binding CspA-related proteins.
• molecular chaperones (DnaK/GroEL/GroES/Clp/TF) preserves protein folding and proteostasis in the cold

  Chaperone/protease systems counter cold-slowed folding and misfolding risk.

  • DOI:10.3389/fmicb.2023.1197797 Psychrophiles constitutively synthesize molecular chaperones; Clp/GroEL/DnaK/GroES/TF upregulated during cold shock.
• compatible solutes (glycine betaine/trehalose/glycerol) stabilizes protein and membrane stabilization

  Osmolytes lower freezing damage and stabilize proteins and membranes.

  • DOI:10.3389/fmicb.2023.1197797 Accumulation of compatible osmolytes prevents cell shrinkage, lowers cytoplasmic freezing point, and stabilizes proteins and membranes.
• ice-binding/antifreeze proteins inhibits ice-crystal growth/recrystallization RO:0002212

  AFPs/IBPs bind ice and inhibit ice-crystal growth and recrystallization.

  • DOI:10.3389/fmicb.2023.1197797 AFPs bind ice, inhibit ice-crystal growth, produce thermal hysteresis, and show IRI activity.