ArticleGenetics2002
Defects in SPT16 or POB3 (yFACT) in Saccharomyces cerevisiae cause dependence on the Hir/Hpc pathway: polymerase passage may degrade chromatin structure.
Article in Genetics, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 107 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
107 citing papers in PubMed, 1 citations in OpenAlex.
- Keeping it centered: decoding the activities that regulate yeast histone H3 variant Cse4 and confine it to centromeres.Frontiers in cell and developmental biology · 2026Review
- Review
- Multilevel interrogation of H3.3 reveals a primordial role in transcription regulation.Epigenetics & chromatin · 2023Article
- Article
- H2A mono-ubiquitination differentiates FACT's functions in nucleosome assembly and disassembly.Nucleic acids research · 2022Article
- Histone chaperone FACT complex inhibitor CBL0137 interferes with DNA damage repair and enhances sensitivity of medulloblastoma to chemotherapy and radiation.Cancer letters · 2021Article
- Distinct associations of the Saccharomyces cerevisiae Rad9 protein link Mac1-regulated transcription to DNA repair.Current genetics · 2020Article
- Synergy of Hir1, Ssn6, and Snf2 global regulators is the functional determinant of a Mac1 transcriptional switch in S. cerevisiae copper homeostasis.Current genetics · 2019Article
- Structure of transcribing RNA polymerase II-nucleosome complex.Nature communications · 2018Article
- FACT complex gene duplicates exhibit redundant and non-redundant functions in C. elegans.Developmental biology · 2018Article
- A Genome-Wide Screen Reveals a Role for the HIR Histone Chaperone Complex in Preventing Mislocalization of Budding Yeast CENP-A.Genetics · 2018Article
- The histone chaperone FACT modulates nucleosome structure by tethering its components.Life science alliance · 2018Article
- Structure and function of the histone chaperone FACT - Resolving FACTual issues.Biochimica et biophysica acta. Gene regulatory mechanisms · 2018Review
- The elongation factor Spn1 is a multi-functional chromatin binding protein.Nucleic acids research · 2018Article
- Stabilization of Nucleosomes by Histone Tails and by FACT Revealed by spFRET Microscopy.Cancers · 2017Article
- Large-scale ATP-independent nucleosome unfolding by a histone chaperone.Nature structural & molecular biology · 2016Article
- Establishment of a promoter-based chromatin architecture on recently replicated DNA can accommodate variable inter-nucleosome spacing.Nucleic acids research · 2016Article
- The Modifier of Transcription 1 (Mot1) ATPase and Spt16 Histone Chaperone Co-regulate Transcription through Preinitiation Complex Assembly and Nucleosome Organization.The Journal of biological chemistry · 2016Article
- Integrated molecular mechanism directing nucleosome reorganization by human FACT.Genes & development · 2016Article
- Translation of Genotype to Phenotype by a Hierarchy of Cell Subsystems.Cell systems · 2016Article
47 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Spt16/Cdc68, Pob3, and Nhp6 collaborate in vitro and in vivo as the yeast factor SPN, which is homologous to human FACT. SPN/FACT complexes mediate passage of polymerases through nucleosomes and are important for both transcription and replication. An spt16 mutation was found to be intolerable when combined with a mutation in any member of the set of functionally related genes HIR1, HIR2/SPT1, HIR3/HPC1, or HPC2. Mutations in POB3, but not in NHP6A/B, also display strong synthetic defects with hir/hpc mutations. A screen for other mutations that cause dependence on HIR/HPC genes revealed genes encoding members of the Paf1 complex, which also promotes transcriptional elongation. The Hir/Hpc proteins affect the expression of histone genes and also promote normal deposition of nucleosomes; either role could explain an interaction with elongation factors. We show that both spt16 and pob3 mutants respond to changes in histone gene numbers, but in opposite ways, suggesting that Spt16 and Pob3 each interact with histones but perhaps with different subsets of these proteins. Supporting this, spt16 and pob3 mutants also display different sensitivities to mutations in the N-terminal tails of histones H3 and H4 and to mutations in enzymes that modulate acetylation of these tails. Our results support a model in which SPN/FACT has two functions: it disrupts nucleosomes to allow polymerases to access DNA, and it reassembles the nucleosomes afterward. Mutations that impair the reassembly activity cause chromatin to accumulate in an abnormally disrupted state, imposing a requirement for a nucleosome reassembly function that we propose is provided by Hir/Hpc proteins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.