ArticleNucleic acids research2004
Domain organization of the yeast histone chaperone FACT: the conserved N-terminal domain of FACT subunit Spt16 mediates recovery from replication stress.
Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 50 citations in OpenAlex.
- Article
- The fly homolog of SUPT16H, a gene associated with neurodevelopmental disorders, is required in a cell-autonomous fashion for cell survival.Human molecular genetics · 2023Article
- The FACT complex facilitates expression of lysosomal and antioxidant genes through binding to TFEB and TFE3.Autophagy · 2022Article
- The fork protection complex recruits FACT to reorganize nucleosomes during replication.Nucleic acids research · 2022Article
- FACT interacts with Set3 HDAC and fine-tunes GAL1 transcription in response to environmental stimulation.Nucleic acids research · 2021Article
- The role of FACT in managing chromatin: disruption, assembly, or repair?Nucleic acids research · 2020Review
- Histone chaperone FACT is essential to overcome replication stress in mammalian cells.Oncogene · 2020Article
- Histone Chaperone FACT and Curaxins: Effects on Genome Structure and Function.Journal of cancer metastasis and treatment · 2019Article
- Structure and function of the histone chaperone FACT - Resolving FACTual issues.Biochimica et biophysica acta. Gene regulatory mechanisms · 2018Review
- H3K4 Methylation Dependent and Independent Chromatin Regulation byG3 (Bethesda, Md.) · 2018Article
- Proteomic analysis of Potentilla fruticosa L. leaves by iTRAQ reveals responses to heat stress.PloS one · 2017Article
- Structure of the human histone chaperone FACT Spt16 N-terminal domain.Acta crystallographica. Section F, Structural biology communications · 2016Article
- The FACT complex interacts with the E3 ubiquitin ligase Psh1 to prevent ectopic localization of CENP-A.Genes & development · 2014Article
- Article
- Structure of the Spt16 middle domain reveals functional features of the histone chaperone FACT.The Journal of biological chemistry · 2013Article
- Identification of Mutant Versions of the Spt16 Histone Chaperone That Are Defective for Transcription-Coupled Nucleosome Occupancy in Saccharomyces cerevisiae.G3 (Bethesda, Md.) · 2012Article
- The role of FACT in making and breaking nucleosomes.Biochimica et biophysica acta · 2012Article
- Histone chaperone FACT coordinates nucleosome interaction through multiple synergistic binding events.The Journal of biological chemistry · 2011Article
- The histone chaperone facilitates chromatin transcription (FACT) protein maintains normal replication fork rates.The Journal of biological chemistry · 2011Article
- Insight into the mechanism of nucleosome reorganization from histone mutants that suppress defects in the FACT histone chaperone.Genetics · 2011Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 FACT subunit Pob3, the yeast homolog of the metazoan SSRP1 protein. Our findings suggest that each FACT subunit is a multidomain protein, and that FACT integrity depends on Pob3 interactions with the Spt16 Mid domain. The conserved Spt16 N-terminal domain (NTD) is shown to be without essential function during normal growth, but becomes important under conditions of replication stress. Genetic interactions suggest that some functions carried out by the Spt16 NTD may be partially redundant within FACT.
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