temperature optimum high

Edge evidence

• hot environment selects for thermophile protein thermostability METPO:2007401

  Hot environments select for thermophile thermostable machinery.

  • DOI:10.1016/s0300-9629(97)00003-0 adapted to environments of high temperature Supports hot environments as the context for thermophile optima.
• thermophile protein thermostability produces temperature optimum high METPO:2000202

  Thermophile thermostability yields a >40 °C optimum.

  • DOI:10.1128/MMBR.65.1.1-43.2001 resistant to irreversible inactivation at high temperatures Supports thermostability as the mechanism producing thermophile optima.
• temperature optimum high is a temperature optimum rdfs:subClassOf

  Temperature optimum high 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 >40 °C optimum as a value within the temperature-optimum distribution.
• reverse gyrase positively regulates positive DNA supercoiling

  Reverse gyrase introduces positive supercoils into DNA, a thermophile hallmark.

  • DOI:10.1264/jsme2.me23087 Reverse gyrase introduces positive supercoils into DNA and is a hallmark of many thermophiles.
• positive DNA supercoiling reduces DNA melting at high temperature METPO:2000017

  Positive supercoiling limits DNA melting and prevents thermal denaturation.

  • DOI:10.1264/jsme2.me23087 Reverse gyrase / positive supercoiling proposed to limit DNA melting and prevent thermal denaturation.
• nucleoid-associated proteins increases genome thermostability RO:0002213

  Nucleoid-associated proteins enhance DNA/genome thermostability.

  • DOI:10.1264/jsme2.me23087 NAPs affect 3D genome organization and enhance DNA thermostability; abundance correlates with growth temperature.
• small heat shock proteins prevents heat-induced protein aggregation RO:0002212

  Small heat shock proteins bind denaturing proteins to prevent heat-induced aggregation.

  • DOI:10.1128/mbio.03593-22 Small HSPs bind denaturing proteins and protect them from aggregation under heat stress.
• thermosome (group II chaperonin) refolds refolding of denatured proteins

  Thermosome refolds denatured proteins in an ATP-dependent manner.

  • DOI:10.1128/mbio.03593-22 Thermosome refolds denatured proteins in an ATP-dependent manner.
• altered membrane lipid composition stabilizes cytoplasmic membrane thermostability

  Altered membrane lipid composition stabilizes the cytoplasmic membrane at high temperature.

  • DOI:10.1128/mbio.03593-22 Heat shock leads to an altered lipid composition of the cytoplasmic membrane; unique membrane composition is a recognized thermophile adaptation.
• hydrophobic and charged amino acid enrichment increases thermophile protein thermostability RO:0002213

  Enrichment in hydrophobic and charged amino acids increases protein thermostability.

  • DOI:10.1128/mbio.02174-23 Thermophiles show enrichment in hydrophobic and charged amino acids contributing to intrinsic protein thermostability.