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FACT (facilitates chromatin transcription, [1] sometimes facilitates chromatin transactions [2] [3]) is a heterodimeric protein complex that affects eukaryotic RNA polymerase II (Pol II) transcription elongation both in vitro and in vivo.It was discovered in 1998 as a factor purified from human cells that was essential for productive, in vitro Pol II transcription on a chromatinized DNA template.

FACT is a histone chaperone that supports transcription through chromatin in vitro, but its in vivo functions are unclear. This study shows that FACT maintains chromatin structure and +1 nucleosome integrity, which stabilizes promoter-proximal pausing and elongation of RNA polymerase II.

The FAcilitates Chromatin Transcription (FACT) complex was originally discovered as a factor that facilitates transcription elongation through nucleosomes in vitro [1].The FACT complex is composed of two subunits, SPT16 (Suppressor of Ty 16) and SSRP1 (Structure Specific Recognition Protein 1) [2].Several early studies using an in vitro transcription assay to analyze purified human FACT from ...

FACT mixed with H3/H4 alone resulted in aggregation, suggesting that binding of an H2A/H2B dimer facilitates the proper interaction of FACT with the H3-H4 tetramer in a ternary complex. They propose a model in which a FACT/H2A/H2B complex interacts with a DNA-bound H3/H4 tetramer, thus forming an intermediate in nucleosome assembly.

The nucleosome, consisting of octamer of core histones, is a barrier for several cellular processes that require access to the naked DNA. The FAcilitates Chromatin Transcription (FACT), a histone chaperone complex, is involved in nucleosome remodeling via eviction or assembly of histones during transcription, replication, and DNA repair.

The human FACT complex is a heterodimer composed of two subunits SPT16 and SSRP1 (Orphanides et al., 1999) (Figure S2A). We investigated the folding and unfolding dynamics of the nucleosome in the presence of the isolated SPT16 and SSRP1 instead of the holo-FACT complex (Figure S2B).

The FACT complex interacts with the E3 ubiquitin ligase Psh1 to prevent ectopic localization of CENP-A. Genes Dev. 2014; 28:1815–1826. [PMC free article] [Google Scholar] 14. Prendergast L., Muller S., Liu Y., Huang H., Dingli F., Loew D., Vassias I., Patel D.J., Sullivan K.F., Almouzni G.. The CENP-T/-W complex is a binding partner of the ...

The facilitates chromatin transcription (FACT) complex is a heterodimeric histone chaperone complex that comprises two core subunits, structure-specific recognition protein 1 (SSRP1) and suppressor of Ty 16 (SUPT16H) (Orphanides et al., 1999).The FACT complex plays a critical role in transcription initiation, transcription elongation, DNA replication, and DNA repair (Carrozza et al., 2003).

FACT is an abundant complex, with about 25,000 heterodimers per haploid yeast cell, or roughly one complex per three nucleosomes . It therefore seems likely that sufficient amounts of FACT would be readily available for any process without recruiting it to specific sites, but the amount of FACT associated with some promoters and ...

The FACT complex facilitates transcription on chromatin templates in vitro, and it has been functionally linked to nucleosomes and putative RNA polymerase II (Pol II) elongation factors. In Saccharomyces cerevisiae cells, FACT specifically associates with active Pol II genes in a TFIIH-dependent manner and travels across the gene with ...

FACT association appears to occur just downstream of the preinitiation complex. To address when FACT associates with the transcription complex, we compared its promoter-proximal distribution to Pol II and other transcription factors at the GAL1-YLR454 locus (Fig. 3A). For Rpb3, Spt16, and Hpr1 (a component of the TREX complex), we arbitrarily ...

The large DNA-binding surface on FACT appears to be protected by the carboxy-terminal domains of both of its subunits, and this inhibition is released by interaction with H2A-H2B, allowing FACT-H2A-H2B to dock onto a complex containing DNA and histones H3 and H4 (ref. 3 ). SPT16 binds nucleosomal DNA and tethers H2A-H2B through its carboxy ...

FACT is an abundant nuclear complex composed of two proteins that are evolutionarily conserved in all eukaryotes. The large subunit, p140h/Spt16, is a mammalian homolog of the yeast Spt16/Cdc68 protein, whereas the smaller subunit, structure-specific recognition protein 1 (SSRP1), is a high mobility group (HMG)–like protein with an N terminus ...

Complex: FACT complex Macromolecular complex annotations are imported from the Complex Portal.These annotations have been derived from physical molecular interaction evidence extracted from the literature and cross-referenced in the entry, or by curator inference from information on homologs in closely related species or by inference from scientific background.

FACT OVERVIEW Forensic assertive community treatment (FACT) is a service delivery model intended for individuals with serious mental illness (SMI) who are involved with the criminal justice system. These individuals may have co-occurring substance use and physical health disorders. Their needs are often complex, and

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Replicative helicase MCM is a novel interacting protein of FACT. (A) FACT-associated complexes were immunoprecipitated from HeLa nuclear extracts (derived from 2 × 10 7 cells) using αSSRP1 mAb 10D1, resolved by and shown on a silver-stained gel (also see Tan and Lee, 2004).Specific SSRP1-interacting protein bands that are absent in the control immunoprecipitates (not shown) were identified ...

that the FACT complex facilitates the transcription of NRF2-target genes and is essential for HCC cells to survive under oxidative stress. Based on this observation, we hypothesized that the FACT complex may play an imperative role in various adaptive responses of cancer cells. Hypoxia (O 2 deprivation) is a common feature of human can-cers.