Core histone lysine acetylation

evidence_span

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experimental_model

Matched cell-type and time-course comparison

exposure

Sulforaphane exposure; serum and time-course comparisons

limitations

Activity assays, protein abundance and substrate acetylation are distinct endpoints; mechanism of their divergence was not established. Erratum PMID 27271518 adds an omitted funding acknowledgment without revising these results.

nutrient_topic

Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study

organism

Human HaCaT keratinocytes and HCT116 colon cancer cells

plain_language

Less enzyme protein did not produce the expected increase in acetylation.

primary_references

[sulforaphane-p25307283] The effect of sulforaphane on histone deacetylase activity in keratinocytes: Differences between in vitro and in vivo analyses. (2015). https://pubmed.ncbi.nlm.nih.gov/25307283/ DOI: 10.1002/mc.22224

tissue_or_cell_type

HDAC activity, protein levels and target acetylation

Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 606–617

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Matched cell-type and time-course comparison · source_derived_draft · unverified_draft

### sulforaphane-histone-acetylation-down Sulforaphane decreased acetylated histone H3, H4 and tubulin markers in the cell comparisons despite reduced HDAC protein levels. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Less enzyme protein did not produce the expected increase in acetylation. organism: Human HaCaT keratinocytes and HCT116 colon cancer cells tissue_or_cell_type: HDAC activity, protein levels and target acetylation experimental_model: Matched cell-type and time-course comparison limitations: Activity assays, protein abundance and substrate acetylation are distinct endpoints; mechanism of their divergence was not established. Erratum PMID 27271518 adds an omitted funding acknowledgment without revising these results. exposure: Sulforaphane exposure; serum and time-course comparisons evidence_span: {"source_cache": "artifacts/sulforaphane-research/25307283.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "cc736d6c2f2dc6c4026bdad0a5835d69ed094775076a2c1606f47020e6783331", "start_char": 0, "end_char": 1504, "text_sha256": "cc736d6c2f2dc6c4026bdad0a5835d69ed094775076a2c1606f47020e6783331"} [sulforaphane-p25307283] The effect of sulforaphane on histone deacetylase activity in keratinocytes: Differences between in vitro and in vivo analyses. (2015). https://pubmed.ncbi.nlm.nih.gov/25307283/ DOI: 10.1002/mc.22224

evidence_span

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experimental_model

Cell exposure, enzyme assays, metabolites and chromatin immunoprecipitation

exposure

Parent SFN, SFN-GSH, SFN-Cys and SFN-NAC; GST inhibition

limitations

High-level HDAC activity was measured without establishing universal isoform inhibition; cell effects are not cancer-treatment outcomes.

nutrient_topic

Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study

organism

Human HEK293 and HCT116 cells

plain_language

The study measured a change to the chemical marks on DNA-packaging proteins.

primary_references

[sulforaphane-p15313918] A novel mechanism of chemoprotection by sulforaphane: inhibition of histone deacetylase. (2004). https://pubmed.ncbi.nlm.nih.gov/15313918/ DOI: 10.1158/0008-5472.can-04-1326

tissue_or_cell_type

Histone deacetylase activity and histone acetylation

Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 593–604

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cell exposure, enzyme assays, metabolites and chromatin immunoprecipitation · source_derived_draft · unverified_draft

### sulforaphane-histone-acetylation-up Sulforaphane exposure increased acetylated histones in HEK293 and HCT116 experiments, including increased acetylated histones at the HCT116 P21 promoter. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The study measured a change to the chemical marks on DNA-packaging proteins. organism: Human HEK293 and HCT116 cells tissue_or_cell_type: Histone deacetylase activity and histone acetylation experimental_model: Cell exposure, enzyme assays, metabolites and chromatin immunoprecipitation limitations: High-level HDAC activity was measured without establishing universal isoform inhibition; cell effects are not cancer-treatment outcomes. exposure: Parent SFN, SFN-GSH, SFN-Cys and SFN-NAC; GST inhibition evidence_span: {"source_cache": "artifacts/sulforaphane-research/15313918.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9478957b1513e25cb47f13d6a1aca0df542fc851d8eb4b9c6394010e90dbe83e", "start_char": 0, "end_char": 1861, "text_sha256": "9478957b1513e25cb47f13d6a1aca0df542fc851d8eb4b9c6394010e90dbe83e"} [sulforaphane-p15313918] A novel mechanism of chemoprotection by sulforaphane: inhibition of histone deacetylase. (2004). https://pubmed.ncbi.nlm.nih.gov/15313918/ DOI: 10.1158/0008-5472.can-04-1326

evidence_span

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experimental_model

Quantitative analysis of acetate metabolism in cultured cells under oxygen and serum limitation

exposure

Exogenous acetate with ACSS2 and ACSS1 manipulation under oxygen and serum limitation

limitations

The quantitative accounting here is the important part and it is a limiting result: demand for two-carbon units far exceeds what exogenous acetate supplies. Cultured cells at a given acetate concentration, which is not a fed human.

nutrient_topic

Acetic acid research collection; topical membership is not evidence of a direct clinical effect, and the ingested acid is recorded separately from the circulating acetate anion. · Acetic acid

organism

Cultured cells

plain_language

Acetate taken in from outside is mostly burned or built into fat; very little of it reaches the histones.

primary_references

[acetate-p28099844] Acetate Recapturing by Nuclear Acetyl-CoA Synthetase 2 Prevents Loss of Histone Acetylation during Oxygen and Serum Limitation. (2017). https://pubmed.ncbi.nlm.nih.gov/28099844/ DOI: 10.1016/j.celrep.2016.12.055

tissue_or_cell_type

Nucleus and cytosol

Acetic acid: the ingested acid, the receptors acetate binds, the acetyl-CoA it becomes, and the acetyl groups that reach histones (2026-09-21) · lines 589–600

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Quantitative analysis of acetate metabolism in cultured cells under oxygen and serum limitation · source_derived_draft · unverified_draft

### acetate-exogenous-acetate-sparing Exogenous acetate uptake is controlled by expression of both ACSS2 and the mitochondrial ACSS1, and the mitochondrial and lipogenic demand for two-carbon acetyl units considerably exceeds the uptake of exogenous acetate, leaving it to only sparingly contribute to histone acetylation. Condition category: normal nutrient_topic: Acetic acid research collection; topical membership is not evidence of a direct clinical effect, and the ingested acid is recorded separately from the circulating acetate anion. plain_language: Acetate taken in from outside is mostly burned or built into fat; very little of it reaches the histones. organism: Cultured cells tissue_or_cell_type: Nucleus and cytosol experimental_model: Quantitative analysis of acetate metabolism in cultured cells under oxygen and serum limitation limitations: The quantitative accounting here is the important part and it is a limiting result: demand for two-carbon units far exceeds what exogenous acetate supplies. Cultured cells at a given acetate concentration, which is not a fed human. exposure: Exogenous acetate with ACSS2 and ACSS1 manipulation under oxygen and serum limitation evidence_span: {"source_cache": "artifacts/acetate-research/28099844.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6df5e8ccde04ad8a222db774f6a8b1e8838ad6a1d918ff84b667d6dde57de188", "start_char": 0, "end_char": 1134, "text_sha256": "6df5e8ccde04ad8a222db774f6a8b1e8838ad6a1d918ff84b667d6dde57de188"} [acetate-p28099844] Acetate Recapturing by Nuclear Acetyl-CoA Synthetase 2 Prevents Loss of Histone Acetylation during Oxygen and Serum Limitation. (2017). https://pubmed.ncbi.nlm.nih.gov/28099844/ DOI: 10.1016/j.celrep.2016.12.055

evidence_span

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experimental_model

Quantitative analysis of acetate metabolism in cultured cells under oxygen and serum limitation

exposure

Exogenous acetate with ACSS2 and ACSS1 manipulation under oxygen and serum limitation

limitations

The quantitative accounting here is the important part and it is a limiting result: demand for two-carbon units far exceeds what exogenous acetate supplies. Cultured cells at a given acetate concentration, which is not a fed human.

nutrient_topic

Acetic acid research collection; topical membership is not evidence of a direct clinical effect, and the ingested acid is recorded separately from the circulating acetate anion. · Acetic acid

organism

Cultured cells

plain_language

An enzyme sitting on the chromatin catches the acetate released when marks are removed, and puts it straight back.

primary_references

[acetate-p28099844] Acetate Recapturing by Nuclear Acetyl-CoA Synthetase 2 Prevents Loss of Histone Acetylation during Oxygen and Serum Limitation. (2017). https://pubmed.ncbi.nlm.nih.gov/28099844/ DOI: 10.1016/j.celrep.2016.12.055

tissue_or_cell_type

Nucleus and cytosol

Acetic acid: the ingested acid, the receptors acetate binds, the acetyl-CoA it becomes, and the acetyl groups that reach histones (2026-09-21) · lines 602–613

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Quantitative analysis of acetate metabolism in cultured cells under oxygen and serum limitation · source_derived_draft · unverified_draft

### acetate-nuclear-acss2-recapture Oxygen and serum limitation increased nuclear localisation of ACSS2, and nuclear ACSS2 recaptures acetate released from histone deacetylation for recycling by histone acetyltransferases, providing evidence for limited equilibration between nuclear and cytosolic acetyl-CoA and demonstrating that ACSS2 retains acetate to maintain histone acetylation. Condition category: normal nutrient_topic: Acetic acid research collection; topical membership is not evidence of a direct clinical effect, and the ingested acid is recorded separately from the circulating acetate anion. plain_language: An enzyme sitting on the chromatin catches the acetate released when marks are removed, and puts it straight back. organism: Cultured cells tissue_or_cell_type: Nucleus and cytosol experimental_model: Quantitative analysis of acetate metabolism in cultured cells under oxygen and serum limitation limitations: The quantitative accounting here is the important part and it is a limiting result: demand for two-carbon units far exceeds what exogenous acetate supplies. Cultured cells at a given acetate concentration, which is not a fed human. exposure: Exogenous acetate with ACSS2 and ACSS1 manipulation under oxygen and serum limitation evidence_span: {"source_cache": "artifacts/acetate-research/28099844.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6df5e8ccde04ad8a222db774f6a8b1e8838ad6a1d918ff84b667d6dde57de188", "start_char": 0, "end_char": 1134, "text_sha256": "6df5e8ccde04ad8a222db774f6a8b1e8838ad6a1d918ff84b667d6dde57de188"} [acetate-p28099844] Acetate Recapturing by Nuclear Acetyl-CoA Synthetase 2 Prevents Loss of Histone Acetylation during Oxygen and Serum Limitation. (2017). https://pubmed.ncbi.nlm.nih.gov/28099844/ DOI: 10.1016/j.celrep.2016.12.055

availability_state

machinery_impairment Imported condition classification; unverified.

cross_nutrient

false

evidence_location

BioC text lines 11, 51; Fig. 2A–B

experimental_model

ACLY and/or AceCS1 siRNA with acetate supplementation

exposure

0, 1 or 5 mM acetate for 24 hours before lysis after siRNA treatment.

limitations

The authors identify this acetate supply as supraphysiologic; it is not a dietary recommendation and does not show rescue of an absent CoA pool. This experiment does not establish a dietary pantothenate threshold or benefit from B5 supplementation.

nutrient_topic

Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. · Pantothenate (vitamin B5)

organism

Homo sapiens

plain_language

A second acetyl-CoA-producing route could compensate when enough acetate was supplied.

primary_references

[b5-met-chromatin2009] ATP-citrate lyase links cellular metabolism to histone acetylation. (2009). https://pubmed.ncbi.nlm.nih.gov/19461003/ DOI: 10.1126/science.1164097

tissue_or_cell_type

HCT116 cells

trigger_kind

machinery_impairment Imported condition classification; unverified.

Pantothenic acid (vitamin B5): coenzyme A, deficiency and nutrient interactions (2026-09-17) · lines 1005–1017

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · ACLY and/or AceCS1 siRNA with acetate supplementation · source_derived_draft · unverified_draft

### b5-met-acetate-acss2-histone-rescue Extracellular acetate restored histone acetylation in ACLY-silenced HCT116 cells in a dose-dependent manner that required AceCS1, now named ACSS2. Condition category: machinery_impairment nutrient_topic: Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. plain_language: A second acetyl-CoA-producing route could compensate when enough acetate was supplied. organism: Homo sapiens tissue_or_cell_type: HCT116 cells experimental_model: ACLY and/or AceCS1 siRNA with acetate supplementation limitations: The authors identify this acetate supply as supraphysiologic; it is not a dietary recommendation and does not show rescue of an absent CoA pool. This experiment does not establish a dietary pantothenate threshold or benefit from B5 supplementation. exposure: 0, 1 or 5 mM acetate for 24 hours before lysis after siRNA treatment. cross_nutrient: false evidence_location: BioC text lines 11, 51; Fig. 2A–B [b5-met-chromatin2009] ATP-citrate lyase links cellular metabolism to histone acetylation. (2009). https://pubmed.ncbi.nlm.nih.gov/19461003/ DOI: 10.1126/science.1164097

availability_state

machinery_impairment Imported condition classification; unverified.

cross_nutrient

true

evidence_location

BioC text lines 11, 17, 51; Fig. 2A,E

experimental_model

ACLY siRNA versus control

exposure

72-hour siRNA treatment.

limitations

Tubulin acetylation was not comparably reduced. This is a source-specific cellular result, not a universal block of protein acetylation. This experiment does not establish a dietary pantothenate threshold or benefit from B5 supplementation.

nutrient_topic

Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. · Pantothenate (vitamin B5)

organism

Homo sapiens

plain_language

Histone acetylation depended partly on this source of acetyl-CoA in colon-cancer cells.

primary_references

[b5-met-chromatin2009] ATP-citrate lyase links cellular metabolism to histone acetylation. (2009). https://pubmed.ncbi.nlm.nih.gov/19461003/ DOI: 10.1126/science.1164097

tissue_or_cell_type

HCT116 cells and acid-extracted histones

trigger_kind

machinery_impairment Imported condition classification; unverified.

Pantothenic acid (vitamin B5): coenzyme A, deficiency and nutrient interactions (2026-09-17) · lines 991–1003

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · ACLY siRNA versus control · source_derived_draft · unverified_draft

### b5-met-acly-hct-histones ACLY silencing reduced acetylation of the core histones assayed in HCT116 cells. Condition category: machinery_impairment nutrient_topic: Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. plain_language: Histone acetylation depended partly on this source of acetyl-CoA in colon-cancer cells. organism: Homo sapiens tissue_or_cell_type: HCT116 cells and acid-extracted histones experimental_model: ACLY siRNA versus control limitations: Tubulin acetylation was not comparably reduced. This is a source-specific cellular result, not a universal block of protein acetylation. This experiment does not establish a dietary pantothenate threshold or benefit from B5 supplementation. exposure: 72-hour siRNA treatment. cross_nutrient: true evidence_location: BioC text lines 11, 17, 51; Fig. 2A,E [b5-met-chromatin2009] ATP-citrate lyase links cellular metabolism to histone acetylation. (2009). https://pubmed.ncbi.nlm.nih.gov/19461003/ DOI: 10.1126/science.1164097

cross_nutrient

true

evidence_location

BioC text line 21; Fig. 3B–C

experimental_model

Serum stimulation with/without glucose and Acly siRNA

exposure

Experimental serum stimulation and glucose withdrawal; no selective pantothenate deprivation.

limitations

Glucose was the experimentally varied fuel. This is not evidence of B5 deficiency; cellular acetyl-CoA sources differ by context. This experiment does not establish a dietary pantothenate threshold or benefit from B5 supplementation.

nutrient_topic

Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. · Pantothenate (vitamin B5)

organism

Mus musculus

plain_language

Glucose supply affected histone acetylation through an acetyl-CoA-producing enzyme in this cell model.

primary_references

[b5-met-chromatin2009] ATP-citrate lyase links cellular metabolism to histone acetylation. (2009). https://pubmed.ncbi.nlm.nih.gov/19461003/ DOI: 10.1126/science.1164097

tissue_or_cell_type

Immortalized mouse embryonic fibroblasts

Pantothenic acid (vitamin B5): coenzyme A, deficiency and nutrient interactions (2026-09-17) · lines 1019–1031

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Serum stimulation with/without glucose and Acly siRNA · source_derived_draft · unverified_draft

### b5-met-glucose-acly-histones Serum-induced histone acetylation in immortalized mouse embryonic fibroblasts depended on glucose availability and was prevented by Acly silencing. Condition category: normal nutrient_topic: Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. plain_language: Glucose supply affected histone acetylation through an acetyl-CoA-producing enzyme in this cell model. organism: Mus musculus tissue_or_cell_type: Immortalized mouse embryonic fibroblasts experimental_model: Serum stimulation with/without glucose and Acly siRNA limitations: Glucose was the experimentally varied fuel. This is not evidence of B5 deficiency; cellular acetyl-CoA sources differ by context. This experiment does not establish a dietary pantothenate threshold or benefit from B5 supplementation. exposure: Experimental serum stimulation and glucose withdrawal; no selective pantothenate deprivation. cross_nutrient: true evidence_location: BioC text line 21; Fig. 3B–C [b5-met-chromatin2009] ATP-citrate lyase links cellular metabolism to histone acetylation. (2009). https://pubmed.ncbi.nlm.nih.gov/19461003/ DOI: 10.1126/science.1164097

evidence_access

Primary abstract

experimental_model

Human colonic-cell metabolic experiments.

limitations

This is a multistep metabolic conversion; no single CoA ligase is assigned without direct evidence.

nutrient_topic

Butyrate collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Butyrate

plain_language

The same carbon source supported both fuel use and adding acetyl marks.

primary_references

The Warburg effect dictates the mechanism of butyrate-mediated histone acetylation and cell proliferation. · 2012 · https://pubmed.ncbi.nlm.nih.gov/23063526/ · DOI 10.1016/j.molcel.2012.08.033

Butyrate: microbial production, fuel use, signaling and nutrient interactions (2026-09-19) · lines 182–188

AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human colonic-cell metabolic experiments. · source_derived_draft · unverified_draft

## butyrate-acetyl-coa The same carbon source supported both fuel use and adding acetyl marks. In the colonic-cell experiments, butyrate metabolism supplied acetyl-CoA for energy metabolism and histone acetyltransferase activity. Model: Human colonic-cell metabolic experiments. Limitations: This is a multistep metabolic conversion; no single CoA ligase is assigned without direct evidence. Evidence access: Primary abstract The Warburg effect dictates the mechanism of butyrate-mediated histone acetylation and cell proliferation. · 2012 · https://pubmed.ncbi.nlm.nih.gov/23063526/ · DOI 10.1016/j.molcel.2012.08.033

evidence_access

Primary abstract

experimental_model

Mouse naive T-cell differentiation, chromatin measurements and colitis experiments.

limitations

Not a claim that butyrate turns every T cell into a Treg or universally suppresses immunity. Correction record: Publisher correction reviewed: Figure 1d upper-right axis identifies Neuropilin-1-positive Foxp3-positive cells; the originally printed negative-marker label was wrong. The notice does not amend the Foxp3 histone-acetylation result cited here. https://www.nature.com/articles/nature13041

nutrient_topic

Butyrate collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Butyrate

plain_language

The surrounding immune signals helped determine which gene program turned on.

primary_references

Commensal microbe-derived butyrate induces the differentiation of colonic regulatory T cells. · 2013 · https://pubmed.ncbi.nlm.nih.gov/24226770/ · DOI 10.1038/nature12721

Butyrate: microbial production, fuel use, signaling and nutrient interactions (2026-09-19) · lines 334–340

AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Mouse naive T-cell differentiation, chromatin measurements and colitis experiments. · source_derived_draft · unverified_draft

## butyrate-foxp3-acetylation The surrounding immune signals helped determine which gene program turned on. Butyrate increased histone H3 acetylation at Foxp3 regulatory regions under Treg-polarizing conditions and promoted Treg differentiation. Model: Mouse naive T-cell differentiation, chromatin measurements and colitis experiments. Limitations: Not a claim that butyrate turns every T cell into a Treg or universally suppresses immunity. Correction record: Publisher correction reviewed: Figure 1d upper-right axis identifies Neuropilin-1-positive Foxp3-positive cells; the originally printed negative-marker label was wrong. The notice does not amend the Foxp3 histone-acetylation result cited here. https://www.nature.com/articles/nature13041 Evidence access: Primary abstract Commensal microbe-derived butyrate induces the differentiation of colonic regulatory T cells. · 2013 · https://pubmed.ncbi.nlm.nih.gov/24226770/ · DOI 10.1038/nature12721

evidence_span

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experimental_model

Drosophila mutagenesis and RNA interference in enteroendocrine cells of the anterior midgut

exposure

Dietary acetate with disruption of a monocarboxylic acid transporter, of histone deacetylation, and of the Tip60 acetyltransferase

limitations

This is a fly study. The mammalian relevance is the authors’ statement that the Tip60-steroid hormone axis is conserved, not a mammalian measurement.

nutrient_topic

Acetic acid research collection; topical membership is not evidence of a direct clinical effect, and the ingested acid is recorded separately from the circulating acetate anion. · Acetic acid

organism

Drosophila

plain_language

Acetate has to be carried inside the cell and turned into a chromatin mark; it is not read at the cell surface.

primary_references

[acetate-p34107298] Microbiota-derived acetate activates intestinal innate immunity via the Tip60 histone acetyltransferase complex. (2021). https://pubmed.ncbi.nlm.nih.gov/34107298/ DOI: 10.1016/j.immuni.2021.05.017

tissue_or_cell_type

Anterior midgut

transport_effect

raises The transporter was required for dietary acetate to reach the intracellular acetyl-CoA route.

transport_pool

the intracellular acetate pool The transporter was required for dietary acetate to reach the intracellular acetyl-CoA route.

Acetic acid: the ingested acid, the receptors acetate binds, the acetyl-CoA it becomes, and the acetyl groups that reach histones (2026-09-21) · lines 693–704

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Drosophila mutagenesis and RNA interference in enteroendocrine cells of the anterior midgut · source_derived_draft · unverified_draft

### acetate-acetate-must-enter Mutagenesis and RNA interference revealed that the putative monocarboxylic acid transporter Tarag was essential for enhancement of immunodeficiency pathway signalling by dietary acetate, and reduced expression of the histone acetyltransferase Tip60 decreased that signalling and blocked rescue by dietary acetate and by other sources of intracellular acetyl-CoA, while interference with histone deacetylation augmented transcription of ecdysone-regulated genes including pathway targets. Condition category: normal nutrient_topic: Acetic acid research collection; topical membership is not evidence of a direct clinical effect, and the ingested acid is recorded separately from the circulating acetate anion. plain_language: Acetate has to be carried inside the cell and turned into a chromatin mark; it is not read at the cell surface. organism: Drosophila tissue_or_cell_type: Anterior midgut experimental_model: Drosophila mutagenesis and RNA interference in enteroendocrine cells of the anterior midgut limitations: This is a fly study. The mammalian relevance is the authors’ statement that the Tip60-steroid hormone axis is conserved, not a mammalian measurement. exposure: Dietary acetate with disruption of a monocarboxylic acid transporter, of histone deacetylation, and of the Tip60 acetyltransferase evidence_span: {"source_cache": "artifacts/acetate-research/34107298.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4e5644412d174b2512ecf9cedea282b022d647b1b8a82f693a8f389da991425a", "start_char": 0, "end_char": 1179, "text_sha256": "4e5644412d174b2512ecf9cedea282b022d647b1b8a82f693a8f389da991425a"} [acetate-p34107298] Microbiota-derived acetate activates intestinal innate immunity via the Tip60 histone acetyltransferase complex. (2021). https://pubmed.ncbi.nlm.nih.gov/34107298/ DOI: 10.1016/j.immuni.2021.05.017