identifier: traitmech:000205 label: heat shock response definition: A stress response in which acute heat stress induces heat-shock proteins that refold or degrade denatured proteins to restore protein homeostasis. definition_source: DOI:10.1007/s12192-016-0727-z trait_category: PHYSIOLOGY term_kind: CLASS mapping_status: PROPOSED parent_traits: - traitmech:000078 synonyms: - synonym_text: heat-shock response synonym_type: EXACT_SYNONYM source: DOI:10.1007/s12192-016-0727-z - synonym_text: HSR synonym_type: RELATED_SYNONYM source: DOI:10.1128/MMBR.00007-08 evidence: - reference: DOI:10.1007/s12192-016-0727-z snippet: they transiently induce a group of genes called heat shock genes (HSGs) which code for heat shock proteins (HSPs) notes: Schumann reviews heat-shock gene induction and heat-shock protein production as the bacterial response to sudden temperature rise. - reference: DOI:10.1007/s12192-016-0727-z snippet: chaperones binding to denatured proteins and allowing refolding to their native state and ATP-dependent proteases degrading denatured proteins notes: Schumann summarizes the two major functional heat-shock protein classes that clear denatured proteins. - reference: DOI:10.1128/MMBR.00007-08 snippet: The heat shock response (HSR) is classically defined as the cellular response to temperature increase notes: Guisbert et al. define the E. coli heat-shock response and review the sigma-32 regulatory model. - reference: DOI:10.1128/MMBR.00007-08 snippet: The rapid upregulation of chaperones and proteases during the HSR restores an appropriate protein-folding environment in the cell notes: Guisbert et al. support protein-folding homeostasis as the primary function of the E. coli sigma-32-mediated heat-shock response. canonical_examples: - taxon_id: NCBITaxon:562 taxon_label: Escherichia coli note: E. coli is a model for the sigma-32-mediated heat-shock response, including heat-shock chaperone and protease upregulation. reference: DOI:10.1128/MMBR.00007-08 - taxon_id: NCBITaxon:1423 taxon_label: Bacillus subtilis note: B. subtilis is a Gram-positive model for heat-shock stimulon regulation by repressor and alternative-sigma branches. reference: DOI:10.1007/s12192-016-0727-z causal_graphs: - graph_id: heat_shock_response_proteostasis title: Heat-shock proteostasis restoration description: Evidence-backed causal sketch linking acute heat shock to protein unfolding, heat-shock protein induction, and restored protein homeostasis. scope_status: MECHANISTIC scope_notes: This graph captures the conserved proteostasis output of the heat-shock response without making the E. coli sigma-32 branch, B. subtilis HrcA/CtsR branches, or other lineage-specific heat-shock regulators universal. nodes: - node_id: heat_shock_response_trait label: heat shock response node_type: TRAIT grounding: traitmech:000205 description: Capacity to induce heat-shock proteins after acute heat stress. - node_id: acute_heat_shock label: acute heat shock node_type: ENVIRONMENTAL_FACTOR description: A sudden upward temperature shift. - node_id: protein_unfolding label: heat-induced protein unfolding node_type: BIOLOGICAL_PROCESS description: Protein unfolding and aggregation triggered by heat shock. - node_id: heat_shock_response_process label: heat-shock response node_type: BIOLOGICAL_PROCESS description: Rapid, transient production of heat-shock proteins after protein unfolding or aggregation. - node_id: heat_shock_chaperones grounding_status: REVIEWED_LABEL_ONLY grounding_notes: Reviewed functional protein set; no single family, complex, or molecular-function term captures all heat-shock-induced chaperones across bacteria. label: heat-shock chaperones node_type: GENE_OR_PROTEIN description: Induced chaperone systems that bind denatured proteins and promote refolding. protein_examples: - uniprot_id: UniProtKB:P0A6Y8 protein_label: Chaperone protein DnaK gene_symbol: dnaK taxon_id: NCBITaxon:83333 taxon_label: Escherichia coli K-12 entry_status: REVIEWED retrieved_on: '2026-09-15' entry_version: 183 sequence_version: 2 role: E. coli K-12 DnaK is an Hsp70 heat-shock chaperone that binds sigma-32 in the chaperone-mediated heat-shock control branch. evidence: - reference: DOI:10.1073/pnas.89.8.3516 snippet: purified sigma 32 bound to DnaK and that this complex was disrupted in the presence of ATP notes: Liberek et al. directly support DnaK as an E. coli heat-shock chaperone that binds the sigma-32 transcription factor. - node_id: atp_dependent_proteases grounding_status: REVIEWED_LABEL_ONLY grounding_notes: Reviewed functional protein set; bacterial ATP-dependent proteases belong to multiple non-equivalent families and complexes. label: ATP-dependent proteases node_type: GENE_OR_PROTEIN description: Proteases that clear denatured proteins or degrade heat-shock regulators during the heat-shock response. protein_examples: - uniprot_id: UniProtKB:P0AAI3 protein_label: ATP-dependent zinc metalloprotease FtsH gene_symbol: ftsH taxon_id: NCBITaxon:83333 taxon_label: Escherichia coli K-12 entry_status: REVIEWED retrieved_on: '2026-09-15' entry_version: 155 sequence_version: 1 role: E. coli K-12 FtsH is an ATP-dependent membrane metalloprotease that degrades the sigma-32 heat-shock transcription factor. evidence: - reference: DOI:10.1002/j.1460-2075.1995.tb07253.x snippet: FtsH catalyzed ATP-dependent degradation of biologically active histidine-tagged sigma 32 notes: Tomoyasu et al. directly support FtsH as the E. coli ATP-dependent protease that degrades sigma-32. - node_id: protein_homeostasis label: protein homeostasis node_type: BIOLOGICAL_PROCESS description: Cellular protein-folding state restored by chaperone refolding and protease degradation of denatured proteins. edges: - subject: acute_heat_shock predicate: causes predicate_id: biolink:causes object: protein_unfolding description: Acute heat shock causes protein unfolding and aggregate formation. evidence: - reference: DOI:10.1007/s12192-016-0727-z snippet: A sudden heat shock results in protein unfolding leading to the formation of protein aggregates notes: Verified against the open PMC full text; heat shock immediately destabilizes cellular proteins. - subject: protein_unfolding predicate: causes predicate_id: biolink:causes object: heat_shock_response_process description: Protein unfolding and aggregation trigger rapid, transient heat-shock protein production. evidence: - reference: DOI:10.1007/s12192-016-0727-z snippet: It responds to protein unfolding, aggregation and damage by the rapid and transient production of HSPs notes: Verified against the open PMC full text; the edge links damaged unfolded proteins to the protective heat-shock response. - subject: heat_shock_response_process predicate: positively regulates predicate_id: RO:0002213 object: heat_shock_chaperones description: The heat-shock response induces chaperones that refold denatured proteins. evidence: - reference: DOI:10.1007/s12192-016-0727-z snippet: chaperones binding to denatured proteins and allowing refolding to their native state notes: Verified against the open PMC full text; chaperones are a major heat-shock protein class. - subject: heat_shock_response_process predicate: positively regulates predicate_id: RO:0002213 object: atp_dependent_proteases description: The heat-shock response induces ATP-dependent proteases that remove denatured proteins. evidence: - reference: DOI:10.1007/s12192-016-0727-z snippet: ATP-dependent proteases degrading denatured proteins notes: Verified against the open PMC full text; ATP-dependent proteases are a major heat-shock protein class. - subject: heat_shock_chaperones predicate: contributes to predicate_id: RO:0002326 object: protein_homeostasis description: Heat-shock chaperones help restore proteostasis by refolding denatured proteins. evidence: - reference: DOI:10.1007/s12192-016-0727-z snippet: chaperones binding to denatured proteins and allowing refolding to their native state notes: Verified against the open PMC full text; induced chaperones support refolding of denatured proteins. - subject: atp_dependent_proteases predicate: contributes to predicate_id: RO:0002326 object: protein_homeostasis description: ATP-dependent proteases help restore proteostasis by degrading denatured proteins. evidence: - reference: DOI:10.1007/s12192-016-0727-z snippet: ATP-dependent proteases degrading denatured proteins notes: Verified against the open PMC full text; induced proteases clear denatured proteins. - subject: protein_homeostasis predicate: confers predicate_id: METPO:2007700 object: heat_shock_response_trait description: Restoration of protein-folding homeostasis realizes the heat-shock-response trait. evidence: - reference: DOI:10.1128/MMBR.00007-08 snippet: restores an appropriate protein-folding environment in the cell notes: Verified against the open PMC full text; Guisbert et al. describe proteostasis restoration as the sigma-32-mediated heat-shock response output. discussions: - discussion_id: heat-shock-response-xref-gap prompt: Resolve exact ontology xrefs for organism-level microbial heat shock response before adding TraitRecord xrefs. kind: CURATION_TODO status: OPEN rationale: GO:0009408 response to heat can ground biological-process nodes but is broader than this organism-level stress response trait. Candidate heat-shock-protein, chaperone, and ATP-dependent-protease terms describe narrower molecular machinery rather than the whole response phenotype. posed_by: codex posed_date: '2026-09-15' curation_history: - timestamp: '2026-09-15T04:58:15Z' curator: codex action: MINTED_TRAITMECH_ID changes: Minted heat shock response as a DOI-backed stress-response TraitRecord after a repository-wide duplicate review covering ignored and hidden files; the local METPO snapshot has only an obsolete heat shock response class and the replacement placeholder is reserved in proposals/metpo_traitmech_v82. llm_assisted: true