ArticleMolecular and cellular biology2001
A bipartite yeast SSRP1 analog comprised of Pob3 and Nhp6 proteins modulates transcription.
Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.
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Who cites it
71 citing papers in PubMed, 131 citations in OpenAlex.
- Beyond Chaperoning: The Multifaceted Role of FACT in Chromatin Transactions.International journal of molecular sciences · 2025Review
- Chromatin regulates alternative polyadenylation via the RNA polymerase II elongation rate.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Insights into Spt6: a histone chaperone that functions in transcription, DNA replication, and genome stability.Trends in genetics : TIG · 2023Review
- FACT regulates pluripotency through proximal and distal regulation of gene expression in murine embryonic stem cells.BMC biology · 2023Article
- Review
- Opposing Roles of FACT for Euchromatin and Heterochromatin in Yeast.Biomolecules · 2023Review
- Article
- The fork protection complex recruits FACT to reorganize nucleosomes during replication.Nucleic acids research · 2022Article
- Electron microscopy analysis of ATP-independent nucleosome unfolding by FACT.Communications biology · 2022Article
- The role of FACT in managing chromatin: disruption, assembly, or repair?Nucleic acids research · 2020Review
- The HMGB chromatin protein Nhp6A can bypass obstacles when traveling on DNA.Nucleic acids research · 2020Article
- The FACT Histone Chaperone: Tuning Gene Transcription in the Chromatin Context to Modulate Plant Growth and Development.Frontiers in plant science · 2020Review
- Histone Chaperone FACT and Curaxins: Effects on Genome Structure and Function.Journal of cancer metastasis and treatment · 2019Article
- Transcription Promotes the Interaction of the FAcilitates Chromatin Transactions (FACT) Complex with Nucleosomes inGenetics · 2018Article
- Mechanism of FACT removal from transcribed genes by anticancer drugs curaxins.Science advances · 2018Article
- Structure and function of the histone chaperone FACT - Resolving FACTual issues.Biochimica et biophysica acta. Gene regulatory mechanisms · 2018Review
- Functional roles of the DNA-binding HMGB domain in the histone chaperone FACT in nucleosome reorganization.The Journal of biological chemistry · 2018Article
- Capturing the Asc1p/Molecular & cellular proteomics : MCP · 2017Article
- Chromatin Controls DNA Replication Origin Selection, Lagging-Strand Synthesis, and Replication Fork Rates.Molecular cell · 2017Article
- Large-scale ATP-independent nucleosome unfolding by a histone chaperone.Nature structural & molecular biology · 2016Article
11 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The FACT complex of vertebrate cells, comprising the Cdc68 (Spt16) and SSRP1 proteins, facilitates transcription elongation on a nucleosomal template and modulates the elongation-inhibitory effects of the DSIF complex in vitro. Genetic findings show that the related yeast (Saccharomyces cerevisiae) complex, termed CP, also mediates transcription. The CP components Cdc68 and Pob3 closely resemble the FACT components, except that the C-terminal high-mobility group (HMG) box domain of SSRP1 is not found in the yeast homolog Pob3. We show here that Nhp6a and Nhp6b, small HMG box proteins with overlapping functions in yeast, associate with the CP complex and mediate CP-related genetic effects on transcription. Absence of the Nhp6 proteins causes severe impairment in combination with mutations impairing the Swi-Snf chromatin-remodeling complex and the DSIF (Spt4 plus Spt5) elongation regulator, and sensitizes cells to 6-azauracil, characteristic of elongation effects. An artificial SSRP1-like protein, created by fusing the Pob3 and Nhp6a proteins, provides both Pob3 and Nhp6a functions for transcription, and competition experiments indicate that these functions are exerted in association with Cdc68. This particular Pob3-Nhp6a fusion protein was limited for certain Nhp6 activities, indicating that its Nhp6a function is compromised. These findings suggest that in yeast cells the Cdc68 partners may be both Pob3 and Nhp6, functioning as a bipartite analog of the vertebrate SSRP1 protein.
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