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Article

Domain organization of the yeast histone chaperone FACT: the conserved N-terminal domain of FACT subunit Spt16 mediates recovery from replication stress.

Nucleic acids research - 1 Jan 2004

O'Donnell Allyson F, Brewster Neil K, Kurniawan Joelius, Minard Laura V, Johnston Gerald C, Singer Richard A

Abstract excerpt

The abundant nuclear complex termed FACT affects several DNA transactions in a chromatin context, including transcription, replication, and repair. Earlier studies of yeast FACT, which indicated the apparent dispensability of conserved sequences at the N terminus of the FACT subunit Cdc68/Spt16, prompted genetic and biochemical studies reported here that suggest the domain organization for Spt16 and the other...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 15520471
DOI: 10.1093/nar/gkh922
PMCID: PMC528806

Genes

SSRP1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Domain organization of the yeast histone chaperone FACT: the conserved N-terminal domain of FACT subunit Spt16 mediates recovery from replication stress.PMID 15520471Read ↗

Mutant versions of the S. cerevisiae transcription elongation factor Spt16 define regions of Spt16 that functionally interact with histone H3.Semantic proximity Read ↗

The FACT chromatin modulator: genetic and structure/function relationships.Semantic proximity Read ↗

The Histone Chaperone FACT Contributes to DNA Replication-Coupled Nucleosome Assembly.Semantic proximity Read ↗

The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins.Semantic proximity Read ↗

New mutant versions of yeast FACT subunit Spt16 affect cell integrity.Semantic proximity Read ↗

Spt16-Pob3 and the HMG protein Nhp6 combine to form the nucleosome-binding factor SPN.Semantic proximity Read ↗

Insight into the mechanism of nucleosome reorganization from histone mutants that suppress defects in the FACT histone chaperone.Semantic proximity Read ↗

FACT, the Bur kinase pathway, and the histone co-repressor HirC have overlapping nucleosome-related roles in yeast transcription elongation.Semantic proximity Read ↗

Defects in SPT16 or POB3 (yFACT) in Saccharomyces cerevisiae cause dependence on the Hir/Hpc pathway: polymerase passage may degrade chromatin structure.Semantic proximity Read ↗

The yeast FACT complex has a role in transcriptional initiation.Semantic proximity Read ↗

Essential histone chaperones collaborate to regulate transcription and chromatin integrity.Semantic proximity Read ↗

POB3 is required for both transcription and replication in the yeast Saccharomyces cerevisiae.Semantic proximity Read ↗

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