FACT complex
A histone chaperone complex that facilitates nucleosome disassembly and reassembly upon DNA or RNA polymerase passage. [GO:0035101]
Synonyms: Facilitates chromatin transcription complex
Components
| Component | Type | Part of / acts on | Grounding | Genes | Stoichiometry | Essential | Role |
|---|---|---|---|---|---|---|---|
| Spt16 FACT subunit | Protein | part of | Reviewed label only (reviewed name; no accession asserted) | SPT16 | UNKNOWN | Large histone-chaperone constituent of the budding-yeast Spt16-Pob3 FACT core.
| |
| Pob3 FACT subunit | Protein | part of | Reviewed label only (reviewed name; no accession asserted) | POB3 | UNKNOWN | Protein constituent of the budding-yeast Spt16-Pob3 FACT core that supplies the SSRP1-related middle domain.
|
Taxonomic distribution
NCBITaxon:4932Saccharomyces cerevisiae — COMMON: Budding yeast is the organism in which Formosa et al. 2001 characterized the Spt16-Pob3 heterodimer that combines with Nhp6 to form the nucleosome-binding factor SPN. [DOI:10.1093/emboj/20.13.3506]
Canonical examples
NCBITaxon:4932Saccharomyces cerevisiae — Formosa et al. 2001 used budding-yeast genetics and protein interaction assays to show that Spt16/Cdc68 and Pob3 form a heterodimeric chromatin factor. [DOI:10.1093/emboj/20.13.3506]
Functions
- nucleosome organization
GO:0034728— FACT reorganizes nucleosomes by facilitating disassembly and reassembly during polymerase passage.GO:0035101GO:0035101 defines the FACT complex as facilitating nucleosome disassembly and reassembly upon polymerase passage.GO:0034728GO:0034728 is the Gene Ontology biological-process term for nucleosome organization.DOI:10.1126/science.1085703Belotserkovskaya et al. 2003 assayed FACT-dependent nucleosome alteration and intrinsic histone chaperone activity.
- DNA-templated transcription elongation
GO:0006354— FACT helps RNA polymerase II elongate transcripts through nucleosomal DNA templates.GO:0006354GO:0006354 is the Gene Ontology biological-process term for DNA-templated transcription elongation.DOI:10.1126/science.1085703Belotserkovskaya et al. 2003 studied FACT activity in RNA polymerase II transcription through nucleosomes.
Mechanism graphs
FACT supports nucleosome reorganization during transcription (FUNCTION)
In Saccharomyces cerevisiae, the Spt16-Pob3 FACT core works with Nhp6 to reorganize nucleosomes and supports RNA polymerase II transcription through nucleosomal templates.
| Subject | Predicate | Object | Evidence |
|---|---|---|---|
| Spt16 FACT subunit | contributes to | FACT complex |
|
| Pob3 FACT subunit | contributes to | FACT complex |
|
| FACT complex | supports | nucleosome organization |
|
| FACT complex | supports | DNA-templated transcription elongation |
|
Discussions
- CURATION_TODO (RESOLVED): Do not model Nhp6 as a core FACT complex constituent. Formosa et al. 2001 reported that Spt16/Cdc68 and Pob3 form a yeast heterodimer and that this heterodimer combines with Nhp6 to form the nucleosome-binding factor SPN, supporting Nhp6 as a DNA-binding cofactor for the yeast SPN activity rather than one of the two FACT core constituents.
- CURATION_TODO (OPEN): Resolve exact source-neutral family groundings for the FACT complex constituents. The curated FACT component labels are yeast gene-name-based classes. This pass verified the gene symbols and the Spt16-Pob3 composition but did not verify exact InterPro, Pfam, NCBIfam or UniProt family CURIEs that should be reused across fungi.
Evidence
GO:0035101Gene Ontology cellular-component term for FACT complex and its Facilitates chromatin transcription complex exact synonym.GO:0008023Gene Ontology cellular-component parent term for transcription elongation factor complexes.GO:0034728Gene Ontology biological-process term for nucleosome organization.GO:0006354Gene Ontology biological-process term for DNA-templated transcription elongation.PMID:12934006PubMed identifier for Belotserkovskaya et al. 2003, the FACT nucleosome-alteration paper cited by GO:0035101.DOI:10.1126/science.1085703DOI for Belotserkovskaya et al. 2003, 'FACT facilitates transcription-dependent nucleosome alteration', verified through NCBI E-utilities.PMID:11432837PubMed identifier for Formosa et al. 2001, the budding-yeast Spt16-Pob3 and Nhp6 SPN paper.DOI:10.1093/emboj/20.13.3506DOI for Formosa et al. 2001, 'Spt16-Pob3 and the HMG protein Nhp6 combine to form the nucleosome-binding factor SPN', verified through NCBI E-utilities.
Curation history
2026-09-26T06:31:20Zcodex · CREATED_RECORD — Scaffolded by scripts/new_record.py2026-09-26T06:32:31Zcodex · EXPANDED_RECORD — Added FACT exact synonymy, transcription-elongation-factor-complex parentage, two budding-yeast FACT constituent rows, yeast scope, nucleosome organization and transcription elongation functions, GO/PubMed/DOI evidence, a nonmechanistic function graph, a resolved Nhp6 boundary discussion, and a FACT subunit-grounding TODO.