ArticleEukaryotic cell2013
The carboxyl terminus of Rtt109 functions in chaperone control of histone acetylation.
Article in Eukaryotic cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 23 citations in OpenAlex.
- Strategic targeting of Cas9 nickase expands tandem gene arrays.Cell genomics · 2025Article
- Histone post-translational modification and the DNA damage response.Genes & diseases · 2023Review
- Suppressor mutations that make the essential transcription factor Spn1/Iws1 dispensable in Saccharomyces cerevisiae.Genetics · 2022Article
- Rtt109 slows replication speed by histone N-terminal acetylation.Genome research · 2021Article
- Stoichiometry of Rtt109 complexes with Vps75 and histones H3-H4.Life science alliance · 2020Article
- Two factor authentication: Asf1 mediates crosstalk between H3 K14 and K56 acetylation.Nucleic acids research · 2019Article
- Modulation of azole sensitivity and filamentation by GPI15, encoding a subunit of the first GPI biosynthetic enzyme, in Candida albicans.Scientific reports · 2019Article
- Multisite Substrate Recognition in Asf1-Dependent Acetylation of Histone H3 K56 by Rtt109.Cell · 2018Article
- Functional Analysis of Hif1 Histone Chaperone inG3 (Bethesda, Md.) · 2018Article
- Structural characterization of the Asf1-Rtt109 interaction and its role in histone acetylation.Nucleic acids research · 2018Article
- 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
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- Regulation of histone gene transcription in yeast.Cellular and molecular life sciences : CMLS · 2014Review
- Histone-modifying enzymes, histone modifications and histone chaperones in nucleosome assembly: Lessons learned from Rtt109 histone acetyltransferases.Critical reviews in biochemistry and molecular biologyReview
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
Rtt109 is a fungal histone acetyltransferase (HAT) that catalyzes histone H3 acetylation functionally associated with chromatin assembly. Rtt109-mediated H3 acetylation involves two histone chaperones, Asf1 and Vps75. In vivo, Rtt109 requires both chaperones for histone H3 lysine 9 acetylation (H3K9ac) but only Asf1 for full H3K56ac. In vitro, Rtt109-Vps75 catalyzes both H3K9ac and H3K56ac, whereas Rtt109-Asf1 catalyzes only H3K56ac. In this study, we extend the in vitro chaperone-associated substrate specificity of Rtt109 by showing that it acetylates vertebrate linker histone in the presence of Vps75 but not Asf1. In addition, we demonstrate that in Saccharomyces cerevisiae a short basic sequence at the carboxyl terminus of Rtt109 (Rtt109C) is required for H3K9ac in vivo. Furthermore, through in vitro and in vivo studies, we demonstrate that Rtt109C is required for optimal H3K56ac by the HAT in the presence of full-length Asf1. When Rtt109C is absent, Vps75 becomes important for H3K56ac by Rtt109 in vivo. In addition, we show that lysine 290 (K290) in Rtt109 is required in vivo for Vps75 to enhance the activity of the HAT. This is the first in vivo evidence for a role for Vps75 in H3K56ac. Taken together, our results contribute to a better understanding of chaperone control of Rtt109-mediated H3 acetylation.
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