homeoviscous adaptation

traitmech:000208 · CLASS · PROPOSED

A stress response in which an organism remodels membrane lipid composition to maintain a functional membrane viscosity and fluidity when temperature changes perturb lipid packing.

Trait evidence (4)

  • DOI:10.1146/annurev-micro-091313-103612
    termed homeoviscous adaptation

    de Mendoza reviews the temperature-driven bacterial membrane remodeling response and names it homeoviscous adaptation.

  • DOI:10.1128/spectrum.03925-23
    Upon temperature decrease, the membrane rigidifies and increases in thickness, resulting in activation of the kinase-dominant state of DesK

    Sidarta et al. support membrane rigidification and thickening as proximal physical triggers in the Bacillus subtilis DesK/DesR homeoviscous-adaptation model.

  • DOI:10.1038/s41467-024-53677-5
    hard-wired parameters calibrate the system to generate membrane compositions that maintain constant fluidity

    Hoogerland et al. directly support E. coli temperature adaptation through a fatty-acid synthesis control system that maintains membrane fluidity.

  • DOI:10.1038/s41467-024-53677-5
    restores optimal membrane fluidity within a single generation

    Hoogerland et al. directly connect the E. coli fatty-acid branchpoint valve and transcriptional feedback to rapid membrane-fluidity restoration after temperature shock.

Membrane-fluidity homeostasis by lipid remodeling

Evidence-backed causal sketch linking temperature-driven membrane rigidification to homeoviscous lipid remodeling and restored membrane fluidity.

MECHANISTIC · This graph captures the conserved membrane-fluidity output of homeoviscous adaptation without making the Bacillus DesK/DesR two-component branch, E. coli FabI/FabB metabolic valve, or any single lipid species universal across microbes.

Membrane-fluidity homeostasis by lipid remodeling Interactive directed graph showing evidence-backed causal relationships for homeoviscous adaptation.

Edge evidence

  • temperature downshift causes membrane rigidification biolink:causes

    A temperature decrease causes the bacterial membrane to rigidify and thicken.

    • DOI:10.1128/spectrum.03925-23 Upon temperature decrease, the membrane rigidifies and increases in thickness Sidarta et al. describe rigidification and thickening as the immediate membrane response to temperature decrease.
  • membrane rigidification positively regulates homeoviscous adaptation RO:0002213

    Membrane rigidification is sensed as the physical input that activates homeoviscous lipid remodeling.

    • DOI:10.1128/spectrum.03925-23 Upon temperature decrease, the membrane rigidifies and increases in thickness, resulting in activation of the kinase-dominant state of DesK Sidarta et al. support the physical membrane-state trigger through the B. subtilis DesK sensor model.
  • homeoviscous adaptation positively regulates membrane lipid remodeling RO:0002213

    Homeoviscous adaptation increases lipid remodeling routes, including fatty-acyl desaturation, that counteract bilayer ordering.

    • DOI:10.1128/spectrum.03925-23 desaturates the fatty acyl chains, resulting in membrane fluidization and concomitant decrease of bilayer thickness Sidarta et al. support Des-mediated fatty-acyl desaturation as a concrete B. subtilis homeoviscous remodeling branch.
  • FabI/FabB branchpoint enzymes regulates membrane lipid remodeling RO:0002211

    The E. coli FabI/FabB branchpoint valve allocates fatty-acid synthesis flux between saturated and unsaturated membrane-lipid routes.

    • DOI:10.1038/s41467-024-53677-5 A first element of this regulatory system is a temperature-sensitive metabolic valve that allocates flux between the saturated and unsaturated fatty acid synthesis pathways via the branchpoint enzymes FabI and FabB Hoogerland et al. support the E. coli FabI/FabB branchpoint valve as a regulator of flux between saturated and unsaturated fatty-acid synthesis.
  • membrane lipid remodeling regulates membrane fluidity RO:0002211

    Temperature-dependent membrane lipid remodeling maintains membrane fluidity near a functional setpoint.

    • DOI:10.1038/s41467-024-53677-5 hard-wired parameters calibrate the system to generate membrane compositions that maintain constant fluidity Hoogerland et al. show that the E. coli fatty-acid synthesis system generates temperature-specific membrane compositions that maintain fluidity.
  • membrane fluidity contributes to homeoviscous adaptation RO:0002326

    Restoration of optimal membrane fluidity is the physiological output of homeoviscous adaptation.

    • DOI:10.1038/s41467-024-53677-5 restores optimal membrane fluidity within a single generation Hoogerland et al. directly connect the homeoviscous fatty-acid control system to rapid fluidity restoration.

Protein and taxon examples

Graph nodeProteinTaxonUniProt statusRole and evidence
FabI/FabB branchpoint enzymes UniProtKB:P0AEK4
Enoyl-[acyl-carrier-protein] reductase [NADH] FabI (fabI)
Escherichia coli K-12
NCBITaxon:83333
REVIEWED
retrieved 2026-09-15 · entry v161 · sequence v2

E. coli K-12 FabI catalyzes enoyl-ACP reduction in fatty-acid elongation and participates in the FabI/FabB metabolic valve that allocates flux between saturated and unsaturated fatty-acid synthesis during homeoviscous adaptation.

  • https://rest.uniprot.org/uniprotkb/P0AEK4.json Involved in the elongation cycle of fatty acid which are used in the lipid metabolism Verified FabI identity and fatty-acid elongation role against the live UniProt REST entry for P0AEK4 retrieved on 2026-09-15.
  • DOI:10.1038/s41467-024-53677-5 via the branchpoint enzymes FabI and FabB Hoogerland et al. place FabI in the temperature-sensitive E. coli fatty-acid branchpoint valve.
FabI/FabB branchpoint enzymes UniProtKB:P0A953
3-oxoacyl-[acyl-carrier-protein] synthase 1 (fabB)
Escherichia coli K-12
NCBITaxon:83333
REVIEWED
retrieved 2026-09-15 · entry v155 · sequence v1

E. coli K-12 FabB elongates acyl-ACP substrates in fatty-acid biosynthesis and participates in the FabI/FabB metabolic valve that allocates flux between saturated and unsaturated fatty-acid synthesis during homeoviscous adaptation.

  • https://rest.uniprot.org/uniprotkb/P0A953.json Catalyzes a key reaction in unsaturated fatty acid (UFA) synthesis Verified FabB identity and unsaturated fatty-acid synthesis role against the live UniProt REST entry for P0A953 retrieved on 2026-09-15.
  • DOI:10.1038/s41467-024-53677-5 via the branchpoint enzymes FabI and FabB Hoogerland et al. place FabB in the temperature-sensitive E. coli fatty-acid branchpoint valve.

Provenance

Identifier source
TraitMech local identifier
Definition source
DOI:10.1039/d4cc03114h

Synonyms (2)

  • homoviscous adaptation EXACT_SYNONYM · DOI:10.1146/annurev-micro-091313-103612
  • HVA RELATED_SYNONYM · DOI:10.1039/d4cc03114h

kg-microbe context

No kg-microbe node embedding matched this record in the 2026-04-25 deepwalk.

Canonical examples (2)

Organisms cited as exemplars of this trait. Taxon ids are NCBITaxon and link out to the NCBI record.

  • Escherichia coli NCBITaxon:562 DOI:10.1038/s41467-024-53677-5 E. coli rapidly restores membrane fluidity after temperature shock through a FabI/FabB branchpoint valve coupled to transcriptional feedback.
  • Bacillus subtilis NCBITaxon:1423 DOI:10.1128/spectrum.03925-23 B. subtilis is the model organism for DesK/DesR membrane thickness sensing and Des-mediated fatty-acyl-chain desaturation during cold-induced homeoviscous adaptation.

Discussions and Knowledge Gaps (1)

Open questions attached to this trait. Seeded by just knowledge-gap-scan and curated; see the corpus-wide index.

Resolve an exact external ontology class for organism-level homeoviscous adaptation before adding a TraitRecord xref.

CURATION TODO OPEN homeoviscous-adaptation-xref-gap · raised by codex · 2026-09-15

Not yet attached to a section of this record — a curator sets attaches_to (e.g. causal_graphs#some_edge) so the gap shows beside the mechanism it concerns.

No exact GO, PATO, or METPO class is present in the pinned local snapshot for homeoviscous adaptation. Related lipid metabolism, fatty-acid desaturation, membrane-fluidity, and cold-response terms are narrower, broader, or shifted from the whole-organism membrane-acclimation trait.

Curation history

  1. · MINTED_TRAITMECH_ID · codex

    Minted homeoviscous adaptation as a DOI-backed stress-response TraitRecord after a repository-wide duplicate review covering ignored and hidden files; the local METPO snapshot has no exact homeoviscous-adaptation class and the replacement placeholder is reserved in proposals/metpo_traitmech_v85.

  2. · ADD_PROTEIN_EXAMPLES · codex

    Added E. coli K-12 FabI and FabB UniProt protein examples to the homeoviscous adaptation causal graph and removed a top-level evidence item whose Maiti review citation had no verbatim snippet.

  3. · NORMALIZED_CAUSAL_NODE_ID · codex

    Renamed the homeoviscous graph node membrane_rigidification to the canonical membrane_rigidity QUALITY node id after PR review found that the retired process-shaped alias had been reintroduced.