ReviewCurrent opinion in structural biology2011
Understanding histone acetyltransferase Rtt109 structure and function: how many chaperones does it take?
Review in Current opinion in structural biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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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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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.
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Who cites it
26 citing papers in PubMed, 42 citations in OpenAlex.
- Tuning epigenetics to enhance cancer virotherapy.Acta pharmaceutica Sinica. B · 2026Review
- Maize unstable factor for orange1 encodes a nuclear protein that affects redox accumulation during kernel development.The Plant cell · 2024Article
- Exploring the Molecular Underpinnings of Cancer-Causing Oncohistone Mutants Using Yeast as a Model.Journal of fungi (Basel, Switzerland) · 2023Review
- Article
- Histone post-translational modification and the DNA damage response.Genes & diseases · 2023Review
- Differential requirements for Gcn5 and NuA4 HAT activities in the starvation-induced versus basal transcriptomes.Nucleic acids research · 2023Article
- Fun30 and Rtt109 Mediate Epigenetic Regulation of the DNA Damage Response Pathway inJournal of fungi (Basel, Switzerland) · 2022Article
- Regulatory Roles of Histone Modifications in Filamentous Fungal Pathogens.Journal of fungi (Basel, Switzerland) · 2022Review
- Review
- Multisite Substrate Recognition in Asf1-Dependent Acetylation of Histone H3 K56 by Rtt109.Cell · 2018Article
- Histone chaperone networks shaping chromatin function.Nature reviews. Molecular cell biology · 2017Review
- The histone chaperone Vps75 forms multiple oligomeric assemblies capable of mediating exchange between histone H3-H4 tetramers and Asf1-H3-H4 complexes.Nucleic acids research · 2016Article
- Optimization of protein samples for NMR using thermal shift assays.Journal of biomolecular NMR · 2016Article
- Divergent Residues Within Histone H3 Dictate a Unique Chromatin Structure in Saccharomyces cerevisiae.Genetics · 2016Article
- Class-IIa Histone Deacetylase Inhibition Promotes the Growth of Neural Processes and Protects Them Against Neurotoxic Insult.Molecular neurobiology · 2015Article
- The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution.Nucleic acids research · 2014Article
- Characterization of two different Asf1 histone chaperones with distinct cellular localizations and functions in Trypanosoma brucei.Nucleic acids research · 2014Article
- Fungus-specific sirtuin HstD coordinates secondary metabolism and development through control of LaeA.Eukaryotic cell · 2013Article
- Characterization of the Pneumocystis carinii histone acetyltransferase chaperone proteins PcAsf1 and PcVps75.Infection and immunity · 2013Article
- The carboxyl terminus of Rtt109 functions in chaperone control of histone acetylation.Eukaryotic cell · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Rtt109 (Regulator of Ty1 Transposition 109) is a fungal-specific histone acetyltransferase required for modification of histone H3 K9, K27 and K56. These acetylations are associated with nascent histone H3 and play an integral role in replication-coupled and repair-coupled nucleosome assembly. Rtt109 is unique among acetyltransferases as it is activated by a histone chaperone; either Vps75 (Vacuolar Protein Sorting 75) or Asf1 (Anti-silencing Function 1). Recent biochemical, structural and genetic studies have shed light on the intricacies of this activation. It is now clear that Rtt109-Asf1 acetylates K56, while Rtt109-Vps75 acetylates K9 and K27. This reinforces that Asf1 and Vps75 activate Rtt109 via distinct molecular mechanisms. Structures of Rtt109-Vps75 further imply that Vps75 positions histone H3 in the Rtt109 active site. These structures however raise questions regarding the stoichiometry of the Rtt109-Vps75 complex. This has ramifications for determining the physiological Rtt109 substrate.
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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.