Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Combined Automated Annotation using Multiple IEA Methods
Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance.
Global analysis of protein localization in budding yeast.
Localization of proteins that are coordinately expressed with Cln2 during the cell cycle.
Global landscape of protein complexes in the yeast Saccharomyces cerevisiae.
Rtt109 is required for proper H3K56 acetylation: a chromatin mark associated with the elongating RNA polymerase II.
Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56.
Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication.
Functional dissection of protein complexes involved in yeast chromosome biology using a genetic interaction map.
Interacting proteins Rtt109 and Vps75 affect the efficiency of non-homologous end-joining in Saccharomyces cerevisiae.
Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109.
Fungal Rtt109 histone acetyltransferase is an unexpected structural homolog of metazoan p300/CBP.
Structural insights into histone H3 lysine 56 acetylation by Rtt109.
Molecular basis for the autoregulation of the protein acetyl transferase Rtt109.
Structure of Vps75 and implications for histone chaperone function.
Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75.
Histone chaperone specificity in Rtt109 activation.
Cooperation between the INO80 complex and histone chaperones determines adaptation of stress gene transcription in the yeast Saccharomyces cerevisiae.
Kinetic mechanism of the Rtt109-Vps75 histone acetyltransferase-chaperone complex.
Defining the budding yeast chromatin-associated interactome.
Structure of the Rtt109-AcCoA/Vps75 complex and implications for chaperone-mediated histone acetylation.
Structure and histone binding properties of the Vps75-Rtt109 chaperone-lysine acetyltransferase complex.
Interaction with the histone chaperone Vps75 promotes nuclear localization and HAT activity of Rtt109 in vivo.
Histone H3K56 acetylation, Rad52, and non-DNA repair factors control double-strand break repair choice with the sister chromatid.
Rtt109 prevents hyper-amplification of ribosomal RNA genes through histone modification in budding yeast.
Expression homeostasis during DNA replication.
Asf1 facilitates dephosphorylation of Rad53 after DNA double-strand break repair.
Structural characterization of the Asf1-Rtt109 interaction and its role in histone acetylation.
Two factor authentication: Asf1 mediates crosstalk between H3 K14 and K56 acetylation.
Histone chaperone exploits intrinsic disorder to switch acetylation specificity.
A role for the Saccharomyces cerevisiae Rtt109 histone acetyltransferase in R-loop homeostasis and associated genome instability.
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Rtt109 prevents DNA-RNA hybrid (R-loop) accumulation by acetylating histone H3 lysines 14 and 23, distinct from its H3K56ac role in replication-coupled nucleosome assembly.
"Rtt109 prevents DNA-RNA hybridization by the acetylation of histone H3 lysines 14 and 23"
The social and structural architecture of the yeast protein interactome.
Falcon deep research report on RTT109 (Saccharomyces cerevisiae)
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Rtt109 is the histone acetyltransferase responsible for histone H3 lysine-56
acetylation (H3K56ac) in budding yeast; loss of RTT109 abolishes detectable
H3K56ac, establishing it as essential for this mark.
"Loss of RTT109 causes “absence of detectable K56 acetylation” in vivo, establishing Rtt109 as essential for H3K56ac"
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Rtt109 transfers an acetyl group from acetyl-CoA to the epsilon-amine of lysine
residues on histone H3, with H3K56 as the dominant in vivo site.
"Rtt109 catalyzes **acetyl transfer from acetyl‑CoA to the ε‑amine of lysine residues on histone H3**, producing acetyl‑lysine and CoA. In budding yeast, its defining and dominant reaction is acetylation of **histone H3 lysine 56 (H3K56ac)**"
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Efficient H3K56 acetylation by Rtt109 requires the histone chaperone cofactors
Asf1 or Vps75, which form functionally distinct complexes; Asf1-linked activity
is especially important for resistance to genotoxic agents.
"Rtt109 forms functional HAT complexes with **Asf1** or **Vps75**; these are **functionally distinct**, with Asf1-linked activity being particularly important for genotoxic resistance"
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Vps75 stimulates the kcat of Rtt109 histone acetylation roughly 100-fold relative
to Rtt109 alone, acting as a high-affinity catalytic activator.
"Vps75 stimulates the **kcat** of histone acetylation by ~**100‑fold** compared with Rtt109 alone"
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The Rtt109-Vps75 complex can also acetylate H3 N-terminal tail lysines, especially
H3K9; VPS75 deletion reduces S-phase H3K9ac by ~60% with only modest effect on
bulk H3K56ac.
"Mass spectrometry and enzymology implicated H3 tail lysines such as **K9** (and other tail sites) as targets of the Rtt109–Vps75 complex, and VPS75 deletion reduced S-phase H3K9ac substantially"
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Asf1 promotes Rtt109 acetylation in the context of H3-H4 substrate presentation
rather than free H3, consistent with a chaperone handoff model for new histones.
"Asf1 promotes acetylation in the context of **H3–H4** substrate presentation (rather than free H3 alone), consistent with a chaperone handoff model for new histones"
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H3K56ac marks newly synthesized H3 during S phase and promotes binding of the
histone deposition factors CAF-1 and Rtt106, linking Rtt109 to replication-coupled
nucleosome assembly.
"H3K56ac marks newly synthesized H3 during S phase and promotes binding of histone deposition factors **CAF-1** and **Rtt106**, linking Rtt109 directly to replication-coupled nucleosome assembly"
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Rtt109-installed H3K56ac promotes chromatin maturation after DNA replication by
enhancing ISWI-family remodelers (yeast Isw1; human SNF2h) that resolve
disorganized nascent chromatin.
"H3K56ac enhances activity of ISWI remodelers (yeast Isw1; human SNF2h) and helps remodel disorganized nascent chromatin; aberrantly low or high levels of H3K56ac perturb maturation and are linked to genome instability"
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rtt109 deletion causes an approximately 9-fold increase in gross chromosomal
rearrangement frequency, consistent with a genome stability role during replication.
"In a foundational *Science* study, **rtt109Δ** caused an approximately **9‑fold increase in gross chromosomal rearrangement** frequency and showed phenotypes consistent with replication-associated DNA damage tolerance defects"
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Rtt109-mediated H3K56 acetylation is required for proper S-phase chromosome domain
positioning, including telomere peripheral localization, indicating nuclear chromatin
action during/after replication.
"H3K56 acetylation is required for S-phase chromosome domain positioning (e.g., telomere peripheral localization), reinforcing that the functional action is on nuclear chromatin during/after replication"
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Although fungal-specific in sequence, Rtt109 is structurally related to metazoan
p300/CBP-type acetyltransferases.
"Although fungal-specific in sequence, Rtt109 is structurally related to metazoan **p300/CBP**-type acetyltransferases, helping explain catalytic architecture while preserving fungal-selective biology"