glycolytic body

cellstructuremech:glycolytic_body · Ribonucleoprotein · Other · Proposed

A membraneless cytoplasmic ribonucleoprotein assembly that concentrates glycolytic enzymes and associated RNAs during hypoxic growth of Saccharomyces cerevisiae. [DOI:10.7554/eLife.48480]

Fuller et al. 2020, Figure 3 supplement 1. Panel A shows Pfk2-, Fba1- or Eno2-GFP puncta (green) with smFISH signals (red) for the indicated yeast RNAs; OLE1 is a negative-enrichment control, not a claimed enriched cargo. Panel B is the no-probe control, and panels C-E summarize transcript counts and positions. Scale bars: 5 micrometers. FLUORESCENCE · *Saccharomyces cerevisiae* (`NCBITaxon:4932`) · Gregory G Fuller, Ting Han, Mallory A Freeberg, James J Moresco, Amirhossein Ghanbari Niaki, Nathan P Roach, John R Yates, Sua Myong, John K Kim; CC BY, via PubMed Central · CC_BY_4_0 · source: PMC PMC7162659.1 fig3s1 · `DOI:10.7554/eLife.48480`

Synonyms: G body; G-body

Part of: GO:0005737 — cytoplasm (no local record)

UniProt location names: UniProt Consortium, CC BY 4.0. Reference label and route sources.

Components

Component	Type	Part of / acts on	Grounding	Genes	Essential	Role
ATP-dependent 6-phosphofructokinase, eukaryotic-type	Protein	part of	`InterPro:IPR009161`	PFK1, PFK2	UNKNOWN	Pfk1 and Pfk2 concentrate in hypoxic G bodies; Pfk2 contributes to recruitment and daughter-cell assembly, but its deletion does not eliminate mother-cell G bodies. `DOI:10.1016/j.celrep.2017.06.082` Figure 1C directly colocalizes Pfk1-GFP with Pfk2-Azurite. Figures 3 and 4 show partial recruitment and cell-lineage-dependent defects, not universal class essentiality.
Fructose-bisphosphate aldolase, class II, yeast/E. coli subtype	Protein	part of	`InterPro:IPR006411`	FBA1	UNKNOWN	Glycolytic enzyme concentrated with phosphofructokinase in the assembly. `DOI:10.1016/j.celrep.2017.06.082` Figure 1C directly colocalizes Fba1-GFP with Pfk2-Azurite under hypoxia.
Enolase	Protein	part of	`InterPro:IPR000941`	ENO2	UNKNOWN	Glycolytic enzyme used as an independent G-body reporter. `DOI:10.1016/j.celrep.2017.06.082` Figure 1A shows hypoxic Eno2 puncta; the proteomic-validation Results explicitly identify Eno2 as a previously validated G-body component. `DOI:10.7554/eLife.48480` Figure 3 and its supplement use Eno2-GFP for RNA colocalization; targeted-RNase Results report loss of Eno2-GFP G bodies.
Pyruvate kinase	Protein	part of	`InterPro:IPR001697`	CDC19	UNKNOWN	Glycolytic enzyme concentrated in hypoxic G bodies; not conflated with heat-induced Cdc19 aggregates. `DOI:10.1016/j.celrep.2017.06.082` Figure 1C colocalizes Cdc19-GFP with Pfk2-Azurite. This evidence is for hypoxia-induced G bodies, not every Cdc19 punctum.
Heat shock protein 70 family	Protein	part of	`InterPro:IPR013126`	SSA1, SSA2, SSE2	UNKNOWN	Resident chaperone-family members; class membership does not establish a shared assembly requirement. `DOI:10.1016/j.celrep.2017.06.082` Proteomic Identification Results and Figure 2C report Ssa1/Ssa2 colocalization in 80-100% of cells and high-frequency Sse2 colocalization. Single-gene phenotypes do not establish family-wide essentiality.
Small heat shock protein	Protein	part of	`InterPro:IPR031107`	HSP26, HSP42	UNKNOWN	Small heat shock proteins directly associated with hypoxic G bodies. `DOI:10.1016/j.celrep.2017.06.082` Proteomic Identification Results and Figure 2C report high-frequency Hsp26 and Hsp42 colocalization with Pfk2-Azurite.
Alpha,alpha-trehalose-phosphate synthase	Protein	part of	`InterPro:IPR012766`	TPS1	UNKNOWN	Variable metabolic constituent represented by Tps1, not the whole trehalose-synthase complex. `DOI:10.1016/j.celrep.2017.06.082` Proteomic Identification Results report Tps1 colocalization in 60% of cells. The measurement is a cell-level localization frequency, not a stoichiometric fraction.
Acetyl-CoA carboxylase	Protein	part of	`InterPro:IPR049076`	ACC1	UNKNOWN	Variable metabolic constituent observed in a subset of hypoxic cells. `DOI:10.1016/j.celrep.2017.06.082` Proteomic Identification Results and Figure 2C report Acc1 colocalization in 27% of cells; no obligatory occupancy or catalytic contribution within G bodies is inferred.
Fatty acid synthase alpha subunit, yeast	Protein	part of	`InterPro:IPR026025`	FAS2	UNKNOWN	Variable constituent represented by the fatty acid synthase alpha subunit, not an assertion that the entire synthase complex is resident. `DOI:10.1016/j.celrep.2017.06.082` Proteomic Identification Results report Fas2 colocalization in 31% of cells, whereas Fas1 foci were adjacent in 12%. These distinct observations are not combined into a whole-complex composition.
RNA	Rna	part of	`SO:0000356`		UNKNOWN	Associated RNA supports G-body assembly and integrity. No single obligatory transcript species, universal RNA stoichiometry or complete RNA-depletion state is established. `DOI:10.7554/eLife.48480` Hypoxic G-body RIP-seq and smFISH demonstrate associated RNAs. G-body-targeted active RNases inhibit nascent formation and fracture preformed bodies; untargeted RNase and inhibited-RNase controls constrain this interpretation. Normoxic PAR-CLIP alone is not localization evidence.

Organism-specific protein examples

Named proteins in which each component's role was established, with the organism the evidence comes from. The component above is the taxon-agnostic family; these are the specific entries behind it.

ATP-dependent 6-phosphofructokinase, eukaryotic-type

Accession	Protein	Gene	Organism	Entry
`UniProtKB:P16861`	ATP-dependent 6-phosphofructokinase subunit alpha	PFK1	Saccharomyces cerevisiae S288C (`NCBITaxon:559292`)	REVIEWED
Role and evidence (2 references) S288C reference-sequence exemplar for the protein studied in BY4741/BY4742-derived yeast; the accession does not assert that the exact reference stock was imaged. `DOI:10.1016/j.celrep.2017.06.082` Figure 1C directly colocalizes Pfk1-GFP with Pfk2-Azurite. Figures 3 and 4 show partial recruitment and cell-lineage-dependent defects, not universal class essentiality. `https://www.uniprot.org/uniprotkb/P16861/entry` Reviewed UniProtKB identity and gene verified live on 2026-10-05; G-body membership comes from the primary microscopy, not the protein annotation.
`UniProtKB:P16862`	ATP-dependent 6-phosphofructokinase subunit beta	PFK2	Saccharomyces cerevisiae S288C (`NCBITaxon:559292`)	REVIEWED
Role and evidence (2 references) S288C reference-sequence exemplar for the protein studied in BY4741/BY4742-derived yeast; the accession does not assert that the exact reference stock was imaged. `DOI:10.1016/j.celrep.2017.06.082` Figure 1C directly colocalizes Pfk1-GFP with Pfk2-Azurite. Figures 3 and 4 show partial recruitment and cell-lineage-dependent defects, not universal class essentiality. `https://www.uniprot.org/uniprotkb/P16862/entry` Reviewed UniProtKB identity and gene verified live on 2026-10-05; G-body membership comes from the primary microscopy, not the protein annotation.

Fructose-bisphosphate aldolase, class II, yeast/E. coli subtype

Accession	Protein	Gene	Organism	Entry
`UniProtKB:P14540`	Fructose-bisphosphate aldolase	FBA1	Saccharomyces cerevisiae S288C (`NCBITaxon:559292`)	REVIEWED
Role and evidence (2 references) S288C reference-sequence exemplar for the protein studied in BY4741/BY4742-derived yeast; the accession does not assert that the exact reference stock was imaged. `DOI:10.1016/j.celrep.2017.06.082` Figure 1C directly colocalizes Fba1-GFP with Pfk2-Azurite under hypoxia. `https://www.uniprot.org/uniprotkb/P14540/entry` Reviewed UniProtKB identity and gene verified live on 2026-10-05; G-body membership comes from the primary microscopy, not the protein annotation.

Enolase

Accession	Protein	Gene	Organism	Entry
`UniProtKB:P00925`	Enolase 2	ENO2	Saccharomyces cerevisiae S288C (`NCBITaxon:559292`)	REVIEWED
Role and evidence (3 references) S288C reference-sequence exemplar for the protein studied in BY4741/BY4742-derived yeast; the accession does not assert that the exact reference stock was imaged. `DOI:10.1016/j.celrep.2017.06.082` Figure 1A shows hypoxic Eno2 puncta; the proteomic-validation Results explicitly identify Eno2 as a previously validated G-body component. `https://www.uniprot.org/uniprotkb/P00925/entry` Reviewed UniProtKB identity and gene verified live on 2026-10-05; G-body membership comes from the primary microscopy, not the protein annotation. `DOI:10.7554/eLife.48480` Figure 3 and its supplement use Eno2-GFP for RNA colocalization; targeted-RNase Results report loss of Eno2-GFP G bodies.

Pyruvate kinase

Accession	Protein	Gene	Organism	Entry
`UniProtKB:P00549`	Pyruvate kinase 1	CDC19	Saccharomyces cerevisiae S288C (`NCBITaxon:559292`)	REVIEWED
Role and evidence (2 references) S288C reference-sequence exemplar for the protein studied in BY4741/BY4742-derived yeast; the accession does not assert that the exact reference stock was imaged. `DOI:10.1016/j.celrep.2017.06.082` Figure 1C colocalizes Cdc19-GFP with Pfk2-Azurite. This evidence is for hypoxia-induced G bodies, not every Cdc19 punctum. `https://www.uniprot.org/uniprotkb/P00549/entry` Reviewed UniProtKB identity and gene verified live on 2026-10-05; G-body membership comes from the primary microscopy, not the protein annotation.

Heat shock protein 70 family

Accession	Protein	Gene	Organism	Entry
`UniProtKB:P10591`	Heat shock protein SSA1	SSA1	Saccharomyces cerevisiae S288C (`NCBITaxon:559292`)	REVIEWED
Role and evidence (2 references) S288C reference-sequence exemplar for the protein studied in BY4741/BY4742-derived yeast; the accession does not assert that the exact reference stock was imaged. `DOI:10.1016/j.celrep.2017.06.082` Proteomic Identification Results and Figure 2C report Ssa1/Ssa2 colocalization in 80-100% of cells and high-frequency Sse2 colocalization. Single-gene phenotypes do not establish family-wide essentiality. `https://www.uniprot.org/uniprotkb/P10591/entry` Reviewed UniProtKB identity and gene verified live on 2026-10-05; G-body membership comes from the primary microscopy, not the protein annotation.
`UniProtKB:P10592`	Heat shock protein SSA2	SSA2	Saccharomyces cerevisiae S288C (`NCBITaxon:559292`)	REVIEWED
Role and evidence (2 references) S288C reference-sequence exemplar for the protein studied in BY4741/BY4742-derived yeast; the accession does not assert that the exact reference stock was imaged. `DOI:10.1016/j.celrep.2017.06.082` Proteomic Identification Results and Figure 2C report Ssa1/Ssa2 colocalization in 80-100% of cells and high-frequency Sse2 colocalization. Single-gene phenotypes do not establish family-wide essentiality. `https://www.uniprot.org/uniprotkb/P10592/entry` Reviewed UniProtKB identity and gene verified live on 2026-10-05; G-body membership comes from the primary microscopy, not the protein annotation.
`UniProtKB:P32590`	Heat shock protein homolog SSE2	SSE2	Saccharomyces cerevisiae S288C (`NCBITaxon:559292`)	REVIEWED
Role and evidence (2 references) S288C reference-sequence exemplar for the protein studied in BY4741/BY4742-derived yeast; the accession does not assert that the exact reference stock was imaged. `DOI:10.1016/j.celrep.2017.06.082` Proteomic Identification Results and Figure 2C report Ssa1/Ssa2 colocalization in 80-100% of cells and high-frequency Sse2 colocalization. Single-gene phenotypes do not establish family-wide essentiality. `https://www.uniprot.org/uniprotkb/P32590/entry` Reviewed UniProtKB identity and gene verified live on 2026-10-05; G-body membership comes from the primary microscopy, not the protein annotation.

Small heat shock protein

Accession	Protein	Gene	Organism	Entry
`UniProtKB:P15992`	Heat shock protein 26	HSP26	Saccharomyces cerevisiae S288C (`NCBITaxon:559292`)	REVIEWED
Role and evidence (2 references) S288C reference-sequence exemplar for the protein studied in BY4741/BY4742-derived yeast; the accession does not assert that the exact reference stock was imaged. `DOI:10.1016/j.celrep.2017.06.082` Proteomic Identification Results and Figure 2C report high-frequency Hsp26 and Hsp42 colocalization with Pfk2-Azurite. `https://www.uniprot.org/uniprotkb/P15992/entry` Reviewed UniProtKB identity and gene verified live on 2026-10-05; G-body membership comes from the primary microscopy, not the protein annotation.
`UniProtKB:Q12329`	Heat shock protein 42	HSP42	Saccharomyces cerevisiae S288C (`NCBITaxon:559292`)	REVIEWED
Role and evidence (2 references) S288C reference-sequence exemplar for the protein studied in BY4741/BY4742-derived yeast; the accession does not assert that the exact reference stock was imaged. `DOI:10.1016/j.celrep.2017.06.082` Proteomic Identification Results and Figure 2C report high-frequency Hsp26 and Hsp42 colocalization with Pfk2-Azurite. `https://www.uniprot.org/uniprotkb/Q12329/entry` Reviewed UniProtKB identity and gene verified live on 2026-10-05; G-body membership comes from the primary microscopy, not the protein annotation.

Alpha,alpha-trehalose-phosphate synthase

Accession	Protein	Gene	Organism	Entry
`UniProtKB:Q00764`	Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 56 kDa subunit	TPS1	Saccharomyces cerevisiae S288C (`NCBITaxon:559292`)	REVIEWED
Role and evidence (2 references) S288C reference-sequence exemplar for the protein studied in BY4741/BY4742-derived yeast; the accession does not assert that the exact reference stock was imaged. `DOI:10.1016/j.celrep.2017.06.082` Proteomic Identification Results report Tps1 colocalization in 60% of cells. The measurement is a cell-level localization frequency, not a stoichiometric fraction. `https://www.uniprot.org/uniprotkb/Q00764/entry` Reviewed UniProtKB identity and gene verified live on 2026-10-05; G-body membership comes from the primary microscopy, not the protein annotation.

Acetyl-CoA carboxylase

Accession	Protein	Gene	Organism	Entry
`UniProtKB:Q00955`	Acetyl-CoA carboxylase	ACC1	Saccharomyces cerevisiae S288C (`NCBITaxon:559292`)	REVIEWED
Role and evidence (2 references) S288C reference-sequence exemplar for the protein studied in BY4741/BY4742-derived yeast; the accession does not assert that the exact reference stock was imaged. `DOI:10.1016/j.celrep.2017.06.082` Proteomic Identification Results and Figure 2C report Acc1 colocalization in 27% of cells; no obligatory occupancy or catalytic contribution within G bodies is inferred. `https://www.uniprot.org/uniprotkb/Q00955/entry` Reviewed UniProtKB identity and gene verified live on 2026-10-05; G-body membership comes from the primary microscopy, not the protein annotation.

Fatty acid synthase alpha subunit, yeast

Accession	Protein	Gene	Organism	Entry
`UniProtKB:P19097`	Fatty acid synthase subunit alpha	FAS2	Saccharomyces cerevisiae S288C (`NCBITaxon:559292`)	REVIEWED
Role and evidence (2 references) S288C reference-sequence exemplar for the protein studied in BY4741/BY4742-derived yeast; the accession does not assert that the exact reference stock was imaged. `DOI:10.1016/j.celrep.2017.06.082` Proteomic Identification Results report Fas2 colocalization in 31% of cells, whereas Fas1 foci were adjacent in 12%. These distinct observations are not combined into a whole-complex composition. `https://www.uniprot.org/uniprotkb/P19097/entry` Reviewed UniProtKB identity and gene verified live on 2026-10-05; G-body membership comes from the primary microscopy, not the protein annotation.

Canonical examples

NCBITaxon:4932 Saccharomyces cerevisiae — Hypoxic yeast G bodies studied using Pfk2-, Fba1- and Eno2-tagged strains, with BY4742 as the untagged immunoprecipitation control. AnaeroPack cultures used YPD or synthetic medium with 5% glucose. This species example does not assert universal occurrence. [DOI:10.7554/eLife.48480]
NCBITaxon:559292 Saccharomyces cerevisiae S288C — Reference lineage for the BY4741-background experiments and reviewed protein exemplars; not a claim that the unmodified S288C stock was imaged. The study also observed Pfk2 puncta in HAP1-wild-type W303, ruling out restriction to the S288C hap1 allele. [DOI:10.1016/j.celrep.2017.06.082]

Functions

Spatial organization of glycolytic enzymes — Concentrates several glycolytic enzymes in a non-membrane-bound cytoplasmic compartment during glucose-supported hypoxic growth.
- DOI:10.1016/j.celrep.2017.06.082 Direct dual-color enzyme colocalization, immunogold TEM and biochemical enrichment support spatial organization. Hypoxia-preconditioned cells with G bodies consume glucose faster than normoxia-preconditioned controls, but preconditioning and Snf1 perturbation have effects beyond the structure.
Contribution to competitive growth under hypoxia — G-body-capable cells have a competitive growth advantage over cells expressing a G-body-targeted active RNase in the tested hypoxic cultures.
- DOI:10.7554/eLife.48480 Growth competition after normoxic preculture includes untargeted MqsR and Pfk2-D348S fusion controls. Targeted RNA degradation may affect local RNAs beyond morphology; this does not prove a single exclusive metabolic mechanism or universal survival requirement.

Physical properties

DIAMETER: 200-500 UO:0000018 (Approximate diameter of electron-dense, non-membrane-bound Pfk2-GFP-labeled bodies in hypoxic S. cerevisiae, measured by immunogold TEM in the 2017 study. Not an invariant size or the Gaussian radius inferred from later fluorescence images.)
- DOI:10.1016/j.celrep.2017.06.082 Hypoxia triggers glycolytic body formation Results describe the approximate TEM diameter and cite Figures 1D and S2C.

Mechanism graphs

RNA-dependent G-body formation during hypoxic growth (ASSEMBLY)

Subject	Predicate	Object	Evidence
Hypoxia with available glucose	promotes	G-body formation	`DOI:10.1016/j.celrep.2017.06.082` Figure 1 and glucose-deprivation controls establish the tested environmental context.
RNA	supports	G-body formation	`DOI:10.7554/eLife.48480` RIP-seq and smFISH establish RNA association; targeted MqsR/RNase A perturbations and activity/targeting controls support the requirement.
Induction of Pfk2-fused active RNase	inhibits	G-body formation	`DOI:10.7554/eLife.48480` Pfk2-MqsR acts dose-dependently; untargeted MqsR does not reproduce the effect and MqsA inhibition rescues formation. RNase A provides a second enzyme test; H12A retains residual activity.

Targeted RNase fractures preformed G bodies (DISASSEMBLY)

Subject	Predicate	Object	Evidence
Induction of G-body-targeted active RNase	promotes	Fragmentation into multiple foci	`DOI:10.7554/eLife.48480` Preformed-body Results distinguish persistent single foci in vector controls from multiple foci following targeted RNase induction.
Preformed glycolytic body	undergoes	Fragmentation into multiple foci	`DOI:10.7554/eLife.48480` Figure 5 and corresponding Results support partial structural disruption, not complete clearance of every body or degradation of every component.

Discussions

INTERPRETATION (RESOLVED): Which broader or related structures must not be merged with the glycolytic body? A local identifier is retained because complete cached OAK label/alias searches and current QuickGO glycolytic searches did not yield an exact cellular-component term. GO:0036464 is a broader class, not identity.
INTERPRETATION (RESOLVED): Does the META-body terminology or engineered recruitment establish an exact synonym or native constituent? Terminology and engineered localization must not inflate the native structural scope.
INTERPRETATION (RESOLVED): Should adjacent proteins, genetic regulators and all proteomics hits be listed as constituents? The 2017 workflow distinguishes 156 candidate hits from microscopy-supported localization.
KNOWLEDGE_GAP (OPEN): Which additional low-frequency or earlier-study candidates are bona fide G-body residents? The inspected Results report more candidates than the conservative high-confidence inventory curated here. Pgi1, Tdh3, Gpm1 and Eno1 form hypoxic puncta with residual cytoplasmic signal, but their dual-label validation and the full supplemental/2013 candidate sets have not been independently audited.
INTERPRETATION (RESOLVED): Do gel-like observations prove a universal liquid-liquid phase-separation mechanism? The 2020 study reports slow fusion, limited fluorescence recovery and incomplete sensitivity to 1,6-hexanediol.
KNOWLEDGE_GAP (OPEN): How does G-body organization change metabolic output independently of pleiotropic perturbations? Hypoxic preconditioning, Snf1 loss and targeted RNA degradation constrain but do not uniquely isolate the causal contribution of compartmentalization. The 2020 Discussion leaves substrate channeling, altered enzyme kinetics and local translation unresolved.

Datasets

Glycolytic body (G body) RIP-sequencing (GSE145881) · NCBI_GEO · TRANSCRIPTOMICS
Organism: Saccharomyces cerevisiae · 6 samples
Metadata-only reference verified from the native GEO SOFT archive on 2026-10-05, matching PMID 32298230 and the paper's Data availability section. No raw reads or processed matrices were reanalyzed. Distinct from normoxic PAR-CLIP evidence.
- https://ftp.ncbi.nlm.nih.gov/geo/series/GSE145nnn/GSE145881/soft/GSE145881_family.soft.gz

Evidence

DOI:10.1016/j.celrep.2017.06.082 Jin et al. 2017; PMID 28746874, PMC5586494.1. Read the defining localization, proteomic-validation, Snf1, metabolism, viability and culture Results/Methods from native JATS. PMC metadata reports not retracted. TDM licensing does not authorize hosting its figures.
DOI:10.7554/eLife.48480 Fuller et al. 2020; PMID 32298230, PMC7162659.1. Read RNA enrichment/localization, targeted-RNase, multivalency, gel-behavior and competition Results plus relevant Methods and Discussion. Native metadata is not retracted and JATS specifies CC BY 4.0. Figure 3 supplement 1 was visually inspected.
DOI:10.1371/journal.pone.0283002 Utsumi et al. 2023. Read the publisher's Introduction and Results/Discussion on engineered peptide recruitment. META body is broader terminology; engineered Adh1 recruitment is not native Adh1 membership evidence.

Curation history

2026-10-05T13:36:52Z codex · CREATED_RECORD — Scaffolded by scripts/new_record.py
2026-10-05T13:40:25Z codex · EXPANDED_RECORD — Added ten component classes, thirteen verified protein exemplars, scoped yeast examples, five mechanistic edges, TEM diameter, licensed microscopy, native GEO metadata and explicit localization/interpretation boundaries.
2026-10-05T13:41:28Z codex · CORRECTED_CITATION_SCOPE — Separated the 2017 Eno2 localization note from the 2020 RNA-localization and RNase evidence at both component and protein-example level.

Source: data/structures/ribonucleoprotein/glycolytic_body.yaml