ArticleNucleic acids research2018
Structural characterization of the Asf1-Rtt109 interaction and its role in histone acetylation.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 22 citations in OpenAlex.
- Epigenetic maintenance of PRC2-repressed chromatin requires RTT109 but not H3K56 acetylation.PLoS genetics · 2026Article
- Exploring the multifaceted roles of histone deacetylase inhibitor vorinostat in the cell growth, mycelial morphology, pigments, and citrinin biosynthesis of Monascus purpureus.Archives of microbiology · 2025Article
- Mechanism of ASF1 engagement by CDAN1.Nature communications · 2025Article
- CODANIN-1 sequesters ASF1 by using a histone H3 mimic helix to regulate the histone supply.Nature communications · 2025Article
- Mechanism of ASF1 Inhibition by CDAN1.bioRxiv : the preprint server for biology · 2024Article
- Research Progress on the Mechanism and Function of Histone Acetylation Regulating the Interaction between Pathogenic Fungi and Plant Hosts.Journal of fungi (Basel, Switzerland) · 2024Review
- Functional analysis of chromatin-associated proteins in Sordaria macrospora reveals similar roles for RTT109 and ASF1 in development and DNA damage response.G3 (Bethesda, Md.) · 2024Article
- Article
- Histone Acetyltransferase Rtt109 Regulates Development, Morphogenesis, and Citrinin Biosynthesis inJournal of fungi (Basel, Switzerland) · 2023Article
- The Role of Chromatin and Transcriptional Control in the Formation of Sexual Fruiting Bodies in Fungi.Microbiology and molecular biology reviews : MMBR · 2022Review
- Tousled-like kinase 2 targets ASF1 histone chaperones through client mimicry.Nature communications · 2022Article
- Article
- Histone Acetylation in the Epigenetic Regulation of Bone Metabolism and Related Diseases.Stem cells international · 2021Review
- The replisome guides nucleosome assembly during DNA replication.Cell & bioscience · 2020Review
- Histone chaperone exploits intrinsic disorder to switch acetylation specificity.Nature communications · 2019Article
- Dynamics and Mechanisms in the Recruitment and Transference of Histone Chaperone CIA/ASF1.International journal of molecular sciences · 2019Article
- Multisite Substrate Recognition in Asf1-Dependent Acetylation of Histone H3 K56 by Rtt109.Cell · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Acetylation of histone H3 at lysine-56 by the histone acetyltransferase Rtt109 in lower eukaryotes is important for maintaining genomic integrity and is required for C. albicans pathogenicity. Rtt109 is activated by association with two different histone chaperones, Vps75 and Asf1, through an unknown mechanism. Here, we reveal that the Rtt109 C-terminus interacts directly with Asf1 and elucidate the structural basis of this interaction. In addition, we find that the H3 N-terminus can interact via the same interface on Asf1, leading to a competition between the two interaction partners. This, together with the recruitment and position of the substrate, provides an explanation of the role of the Rtt109 C-terminus in Asf1-dependent Rtt109 activation.
Indexed as
Identifiers
What OpenQuestion holds
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.