Histone acetyltransferase RTT109 (also KAT11, Regulator of Ty1 transposition protein 109) catalyzes acetylation of newly synthesized histone H3 at lysines 56, 9, 27, 14, and 23 in coordination with histone chaperone cofactors Vps75 and Asf1. RTT109 is required for normal replication-dependent nucleosome assembly and genome stability, as H3K56ac marks nascent DNA and facilitates proper chromatin assembly while preventing double-strand break formation. RTT109 also prevents DNA-RNA hybrid accumulation through H3K14 and H3K23 acetylation. The enzyme exhibits a unique bipartite architecture with N-terminal PAT domain and C-terminal activation domain, undergoes autoacetylation at K290 for catalytic activation, and works with histone chaperones on non-nucleosomal histone H3.
Definition: Any process that decreases the rate, frequency, or extent of R-loop (DNA-RNA hybrid) formation, for example by a chromatin state or histone modification that renders the DNA template less permissive to hybridization with nascent RNA.
Justification: RTT109 loss increases cellular R-loop/DNA-RNA hybrid levels via loss of H3K14 and H3K23 acetylation (PMID:35866610), a function distinct from its defining H3K56ac role in replication-coupled nucleosome assembly and from its separate role in repairing R-loop-associated DNA breaks. No existing GO term captures formation-prevention specifically; the only R-loop process term, GO:0062176 (R-loop processing), is defined as R-loop disassembly, the opposite direction of effect. The mechanism here is chromatin-based β H3K14/H3K23 acetylation rendering the template less permissive to DNA-RNA hybridization β but chromatin organization is the mechanism rather than the parent class. Because the term being proposed is a negative-regulation class, it is parented under GO:0051053 (negative regulation of DNA metabolic process), the nearest existing negative-regulation ancestor, R-loop processing being itself classified in GO as a DNA metabolic process.
Parent term: negative regulation of DNA metabolic process
Supporting Evidence:
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0032931 histone H3K56 acetyltransferase activity | IBA GO_REF:0000033 | ACCEPT | Summary: H3K56 acetyltransferase activity is RTT109 core defining function Reason: RTT109 is sole acetyltransferase for H3K56 on newly synthesized histones. Essential for genome stability - rtt109Ξ shows 3-4 fold elevated spontaneous DSBs and 9-fold higher gross chromosomal rearrangements. Supported by 8 crystal structures revealing active site and multiple biochemical studies. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN001586545 SUPPORTS TRANSFER Fungal RTT109 ancestor seeded by budding yeast RTT109, fission yeast SPBC342.06c, and Candida albicans CAL0000176178 for histone H3K56 acetyltransferase activity; direct budding-yeast evidence is one of the descendant seeds, not a circular donor. Supporting Evidence: PMID:18707894 Saccharomyces cerevisiae Rtt109 is an important class of histone acetyltransferases (HATs), which promote genome stability by directly acetylating newly synthesized histone H3 lysine 56 (H3-K56) through an unknown mechanism PMID:17272722 Rtt109p directly catalyzes this modification in vitro in a manner that is stimulated by Asf1p. |
| GO:0006974 DNA damage response | IBA GO_REF:0000033 | ACCEPT | Summary: DNA damage response through H3K56 acetylation in replication Reason: RTT109 essential for S-phase genome stability. rtt109Ξ cells display 3-4 fold elevated spontaneous DNA damage, severe hypersensitivity to genotoxic agents (MMS, HU, CPT), and impaired nucleosome reassembly at damage sites. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN001586545 SUPPORTS TRANSFER Fungal RTT109 ancestor seeded by budding- and fission-yeast descendants; RTT109's conserved H3K56 acetyltransferase pathway is directly required for genotoxic-stress resistance and genome stability in Saccharomyces cerevisiae. Supporting Evidence: PMID:17272722 Saccharomyces cerevisiae Rtt109p promotes genome stability and resistance to DNA-damaging agents PMID:39631395 Our findings suggest that the RCNA pathway is especially important to repair DSBs arising from nicks in the leading-strand template through acetylation of histone H3K56. |
| GO:0005634 nucleus | IBA GO_REF:0000033 | ACCEPT | Summary: RTT109 localizes to nucleus for replication and chromatin functions Reason: Nucleus is essential cellular compartment for RTT109 acetyltransferase function in DNA replication and nucleosome assembly. Nuclear localization mediated by Vps75 histone chaperone. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN001586545 SUPPORTS TRANSFER Fungal RTT109 ancestor seeded by SGD RTT109 for nuclear localization; the transfer matches the nuclear compartment where Rtt109 acetylates nascent histone H3 during replication and transcription-coupled chromatin regulation. Supporting Evidence: PMID:15282802 Most of these proteins localize to either the nucleus or to sites of cell growth. We are able to assign new cellular component GO terms to ASF2, TOS4, RTT109, YBR070C, YKR090W, YOL007C, YOL019W and YPR174C. |
| GO:0004402 histone acetyltransferase activity | IEA GO_REF:0000120 | ACCEPT | Summary: General histone acetyltransferase activity. The crystal structure of Rtt109 in complex with acetyl-CoA (PDB 3CZ7; Stavropoulos et al. 2008) shows a core PAT domain that binds the acetyl-CoA cofactor and is responsible for acetylating H3K56. Reason: Broad classification encompassing H3K56, K9, K27, K14, K23 acetyltransferase activities on newly synthesized histones. Supporting Evidence: PMID:18719104 Rtt109 is a protein acetyltransferase (PAT) that is responsible for the acetylation of lysine-56 of histone 3 (H3K56) in yeast. PMID:18719104 Here, we present the crystal structure of Rtt109 in complex with acetyl-CoA at a 2.0-A resolution. |
| GO:0005634 nucleus | IEA GO_REF:0000120 | ACCEPT | Summary: Nuclear localization for DNA replication functions Reason: RTT109 functions in nucleus during S-phase DNA replication and chromatin assembly. |
| GO:0006325 chromatin organization | IEA GO_REF:0000002 | ACCEPT | Summary: RTT109 controls chromatin organization through H3K56 acetylation Reason: H3K56 acetylation creates relaxed chromatin structure on nascent DNA during replication and facilitates proper nucleosome positioning and assembly. Multiple biochemical studies confirm chromatin structural changes. |
| GO:0006351 DNA-templated transcription | IEA GO_REF:0000043 | MODIFY | Summary: RTT109 indirectly affects DNA-templated transcription through transcriptional buffering Reason: The UniProt keyword mapping to DNA-templated transcription overshoots because Rtt109 acetylates newly deposited histone H3 and regulates transcriptional homeostasis from chromatin, rather than synthesizing RNA from a DNA template. The adjacent GO:0006355 regulation of DNA-templated transcription row already captures that secondary regulatory role. Proposed replacements: regulation of DNA-templated transcription |
| GO:0006355 regulation of DNA-templated transcription | IEA GO_REF:0000002 | ACCEPT | Summary: Regulation of DNA-templated transcription during replication Reason: RTT109 suppresses transcription at early-replicating genes through H3K56 acetylation, preventing transcriptional upregulation proportional to DNA content increase. |
| GO:0006974 DNA damage response | IEA GO_REF:0000043 | ACCEPT | Summary: DNA damage response annotation consistent with S-phase genome stability role Reason: RTT109 enables cellular response to DNA damage by acetylating H3K56, promoting nucleosome assembly and preventing spontaneous double-strand break formation. |
| GO:0010484 histone H3 acetyltransferase activity | IEA GO_REF:0000002 | ACCEPT | Summary: Histone H3 acetyltransferase activity. The 2.0-A crystal structure of Rtt109 bound to acetyl-CoA (PDB 3CZ7) confirms it is the acetyltransferase responsible for H3K56 acetylation. Reason: RTT109 catalyzes acetylation of histone H3 at multiple lysine residues (K56, K9, K27, K14, K23) depending on histone chaperone cofactor. Supporting Evidence: PMID:18719104 Rtt109 is a protein acetyltransferase (PAT) that is responsible for the acetylation of lysine-56 of histone 3 (H3K56) in yeast. PMID:18719104 Here, we present the crystal structure of Rtt109 in complex with acetyl-CoA at a 2.0-A resolution. |
| GO:0016740 transferase activity | IEA GO_REF:0000043 | MARK AS OVER ANNOTATED | Summary: General transferase activity too broad Reason: Transferase activity (GO:0016740) is extremely broad classification encompassing tens of thousands of enzymes. More specific child terms already annotated (protein-lysine-acetyltransferase, histone acetyltransferase). While technically correct, offers minimal information value per GO guidelines. |
| GO:0061733 protein-lysine-acetyltransferase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Protein-lysine-acetyltransferase activity. The crystal structure of Rtt109 in complex with acetyl-CoA (PDB 3CZ7, ligand ACO; Stavropoulos et al. 2008) directly shows acetyl-CoA bound in the core PAT domain, the cofactor donor for lysine acetylation. Reason: RTT109 catalyzes lysine acetylation using acetyl-CoA as cofactor. EC 2.3.1.48 classification confirmed by enzymatic characterization. Supporting Evidence: PMID:18719104 Rtt109 consists of a core PAT domain, which binds the acetyl-CoA cofactor. PMID:18719104 Here, we present the crystal structure of Rtt109 in complex with acetyl-CoA at a 2.0-A resolution. |
| GO:0005515 protein binding | IPI PMID:16554755 Global landscape of protein complexes in the yeast Saccharom... | REMOVE | Summary: RTT109 binds Vps75 histone chaperone Reason: The Rtt109-Vps75 physical interaction is real, but GO:0005515 is a generic binding term that does not capture the chaperone-stimulated histone acetyltransferase mechanism already represented by RTT109's catalytic and H3 histone acetyltransferase complex annotations. Supporting Evidence: PMID:16554755 Global landscape of protein complexes in the yeast Saccharomyces cerevisiae. |
| GO:0005515 protein binding | IPI PMID:17314980 Functional dissection of protein complexes involved in yeast... | REMOVE | Summary: RTT109 protein interaction with Vps75 Reason: This is another generic GO:0005515 row for a Vps75-associated physical interaction; the protein binding term is uninformative for the specific chaperone-acetyltransferase function and should not be retained as a separate RTT109 molecular function. Supporting Evidence: PMID:17314980 Functional dissection of protein complexes involved in yeast chromosome biology using a genetic interaction map. |
| GO:0005515 protein binding | IPI PMID:18723682 Structure of Vps75 and implications for histone chaperone fu... | REMOVE | Summary: RTT109 protein interaction with Vps75 Reason: The Vps75 association is a well-characterized part of Rtt109 biology, but a generic protein binding annotation adds no specific molecular activity beyond the accepted histone acetyltransferase and H3 histone acetyltransferase complex rows. Supporting Evidence: PMID:18723682 Structure of Vps75 and implications for histone chaperone function. |
| GO:0005515 protein binding | IPI PMID:19172748 Molecular functions of the histone acetyltransferase chapero... | REMOVE | Summary: RTT109 interacts with Vps75 Reason: The cited Rtt109-Vps75 study supports the chaperone-dependent histone acetyltransferase mechanism; GO:0005515 itself is too generic to retain as a functional annotation. Supporting Evidence: PMID:19172748 Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75. |
| GO:0005515 protein binding | IPI PMID:19172749 Histone chaperone specificity in Rtt109 activation. | REMOVE | Summary: Rtt109 can bind Nap1, but only the paralogous Vps75 chaperone stimulates catalysis. Reason: Park et al. found that Nap1 and Vps75 bind Rtt109 with similar affinities but that only Vps75 stimulates Rtt109 enzymatic activity. The Nap1 interaction is therefore not a separate, informative RTT109 molecular function beyond generic protein binding. Supporting Evidence: PMID:19172749 Nap1 and Vps75 interact with histones and Rtt109 with comparable affinities. However, only Vps75 stimulates Rtt109 enzymatic activity. |
| GO:0005515 protein binding | IPI PMID:21179020 Defining the budding yeast chromatin-associated interactome. | REMOVE | Summary: RTT109 interacts with Asf1 Reason: Direct interaction with the Asf1 histone chaperone supports Rtt109's catalytic context, but GO:0005515 is an uninformative physical-association term rather than a specific RTT109 function. Supporting Evidence: PMID:21179020 Defining the budding yeast chromatin-associated interactome. |
| GO:0005515 protein binding | IPI PMID:21256037 Structure of the Rtt109-AcCoA/Vps75 complex and implications... | REMOVE | Summary: RTT109 protein binding interactions documented Reason: The structural Rtt109-Vps75 complex evidence is better represented by the accepted H3 histone acetyltransferase complex and catalytic rows; retaining a duplicate generic protein binding annotation would not add GO-function specificity. Supporting Evidence: PMID:21256037 Structure of the Rtt109-AcCoA/Vps75 complex and implications for chaperone-mediated histone acetylation. |
| GO:0005515 protein binding | IPI PMID:37968396 The social and structural architecture of the yeast protein ... | REMOVE | Summary: Protein binding annotation Reason: This large-scale interactome row asserts only generic protein binding. It does not provide a more informative molecular function than the reviewed Rtt109 histone acetyltransferase and chaperone-complex annotations. Supporting Evidence: PMID:37968396 The social and structural architecture of the yeast protein interactome. |
| GO:0006325 chromatin organization | IDA PMID:18568037 Fungal Rtt109 histone acetyltransferase is an unexpected str... | ACCEPT | Summary: Chromatin organization through replication-dependent acetylation Reason: Direct biochemical demonstration of RTT109 role in organizing newly assembled chromatin. Supporting Evidence: PMID:18568037 Fungal Rtt109 histone acetyltransferase is an unexpected structural homolog of metazoan p300/CBP. |
| GO:0006325 chromatin organization | IMP PMID:18568037 Fungal Rtt109 histone acetyltransferase is an unexpected str... | ACCEPT | Summary: Chromatin organization by RTT109-mediated histone acetylation Reason: IMP evidence: rtt109Ξ cells display disorganized chromatin at replicated regions. Supporting Evidence: PMID:18568037 Fungal Rtt109 histone acetyltransferase is an unexpected structural homolog of metazoan p300/CBP. |
| GO:0006325 chromatin organization | IDA PMID:18707894 Structural insights into histone H3 lysine 56 acetylation by... | ACCEPT | Summary: Chromatin organization mediated by RTT109 Reason: Direct observations of RTT109 effects on chromatin structure. Supporting Evidence: PMID:18707894 Structural insights into histone H3 lysine 56 acetylation by Rtt109. |
| GO:0006325 chromatin organization | IDA PMID:29300933 Structural characterization of the Asf1-Rtt109 interaction a... | ACCEPT | Summary: RTT109 controls chromatin organization during replication Reason: Multiple independent studies confirm role in organizing nascent chromatin. Supporting Evidence: PMID:29300933 Structural characterization of the Asf1-Rtt109 interaction and its role in histone acetylation. |
| GO:0006325 chromatin organization | IDA PMID:31387991 Histone chaperone exploits intrinsic disorder to switch acet... | ACCEPT | Summary: Replication-coupled chromatin organization by RTT109 Reason: H3K56 acetylation essential for proper nucleosome assembly on replicated DNA. Supporting Evidence: PMID:31387991 Histone chaperone exploits intrinsic disorder to switch acetylation specificity. |
| GO:0006335 DNA replication-dependent chromatin assembly | IDA PMID:19172748 Molecular functions of the histone acetyltransferase chapero... | ACCEPT | Summary: DNA replication-dependent chromatin assembly is RTT109 primary function Reason: RTT109 marks nascent DNA through H3K56 acetylation, facilitating H3-H4 transfer to CAF1 for PCNA-coupled nucleosome deposition. Essential for proper replication-dependent nucleosome assembly. Supporting Evidence: PMID:19172748 Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75 file:yeast/RTT109/RTT109-deep-research-falcon.md 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 file:yeast/RTT109/RTT109-deep-research-falcon.md Asf1 presents H3βH4 to **Rtt109** for H3K56 acetylation |
| GO:0006335 DNA replication-dependent chromatin assembly | IDA PMID:21256037 Structure of the Rtt109-AcCoA/Vps75 complex and implications... | ACCEPT | Summary: Replication-dependent chromatin assembly mediated by H3K56 acetylation Reason: RTT109-catalyzed H3K56 acetylation essential step in RCNA pathway coordinating with replication machinery. Supporting Evidence: PMID:21256037 Structure of the Rtt109-AcCoA/Vps75 complex and implications for chaperone-mediated histone acetylation. |
| GO:0006338 chromatin remodeling | IDA PMID:31194870 Two factor authentication: Asf1 mediates crosstalk between H... | ACCEPT | Summary: Chromatin remodeling through H3K56 acetylation weakening DNA-histone contacts Reason: H3K56 acetylation weakens histone-DNA interactions, promoting nucleosome replacement ahead of replication forks and chromatin disassembly during transcription. Supporting Evidence: PMID:31194870 Two factor authentication: Asf1 mediates crosstalk between H3 K14 and K56 acetylation. |
| GO:0000785 chromatin | IDA PMID:21463458 Interaction with the histone chaperone Vps75 promotes nuclea... | ACCEPT | Summary: RTT109 is component of H3 histone acetyltransferase complexes at chromatin Reason: RTT109 physically associates with Vps75 and Asf1 to form active acetyltransferase complexes that localize to chromatin. Supporting Evidence: PMID:21463458 Interaction with the histone chaperone Vps75 promotes nuclear localization and HAT activity of Rtt109 in vivo. |
| GO:0006357 regulation of transcription by RNA polymerase II | IMP PMID:19620280 Cooperation between the INO80 complex and histone chaperones... | KEEP AS NON CORE | Summary: Regulation of RNA polymerase II transcription during S-phase Reason: RTT109 suppresses transcription from newly replicated genes through H3K56 acetylation, preventing transcriptional upregulation during active DNA replication. This is a downstream chromatin consequence of Rtt109 histone acetyltransferase activity rather than a core process. Supporting Evidence: PMID:19620280 Cooperation between the INO80 complex and histone chaperones determines adaptation of stress gene transcription |
| GO:0033554 cellular response to stress | IMP PMID:19620280 Cooperation between the INO80 complex and histone chaperones... | KEEP AS NON CORE | Summary: Cellular response to DNA damage stress Reason: RTT109 enables cell survival to genotoxic stress by acetylating H3 histones, promoting nucleosome assembly and preventing DNA damage. This response-level term is downstream of Rtt109 chromatin assembly activity and is not itself a core Rtt109 process. Supporting Evidence: PMID:19620280 Cooperation between the INO80 complex and histone chaperones determines adaptation of stress gene transcription in the yeast Saccharomyces cerevisiae. |
| GO:0043992 histone H3K9 acetyltransferase activity | IMP PMID:19172748 Molecular functions of the histone acetyltransferase chapero... | ACCEPT | Summary: Histone H3K9 acetyltransferase activity mediated by Rtt109-Vps75 Reason: RTT109-Vps75 complex specifically acetylates H3K9 on newly synthesized histones. H3K9 residue in N-terminal tail region of H3. Supporting Evidence: PMID:19172748 Acetylation of H3 on K56, K9, K14 and K23 were readily observed as the first set of sites modified file:yeast/RTT109/RTT109-deep-research-falcon.md Mass spectrometry and enzymology implicated H3 tail lysines such as **K9** (and other tail sites) as targets of the Rtt109βVps75 complex, and VPS75 deletion reduced S-phase H3K9ac substantially file:yeast/RTT109/RTT109-deep-research-falcon.md VPS75 loss caused ~**60% reduction** in H3K9ac during S phase while having modest effect on bulk H3K56ac |
| GO:0043994 histone H3K23 acetyltransferase activity | IMP PMID:19172748 Molecular functions of the histone acetyltransferase chapero... | ACCEPT | Summary: H3K23 acetyltransferase activity Reason: RTT109 acetylates histone H3K23 residue in coordination with Vps75 on newly synthesized histones. Supporting Evidence: PMID:19172748 Acetylation of H3 on K56, K9, K14 and K23 were readily observed as the first set of sites modified |
| GO:0005515 protein binding | IPI PMID:21454705 Structure and histone binding properties of the Vps75-Rtt109... | REMOVE | Summary: RTT109 protein interaction with Vps75 Reason: The Vps75-Rtt109 structure supports the specific histone chaperone-lysine acetyltransferase complex, while GO:0005515 itself is generic and uninformative as a separate molecular-function row. Supporting Evidence: PMID:21454705 Structure and histone binding properties of the Vps75-Rtt109 chaperone-lysine acetyltransferase complex. |
| GO:0005515 protein binding | IPI PMID:29300933 Structural characterization of the Asf1-Rtt109 interaction a... | REMOVE | Summary: Protein interaction with histone chaperone Reason: The Asf1-Rtt109 interaction is mechanistically meaningful for histone-tail acetylation, but the annotation term here is only generic protein binding and should not be kept as a separate function. Supporting Evidence: PMID:29300933 Structural characterization of the Asf1-Rtt109 interaction and its role in histone acetylation. |
| GO:0043992 histone H3K9 acetyltransferase activity | IDA PMID:21256037 Structure of the Rtt109-AcCoA/Vps75 complex and implications... | ACCEPT | Summary: Histone H3K9 acetyltransferase activity confirmed by direct assay Reason: Biochemical evidence demonstrates RTT109 catalyzes H3K9 acetylation on newly synthesized H3. Supporting Evidence: PMID:21256037 Structure of the Rtt109-AcCoA/Vps75 complex and implications for chaperone-mediated histone acetylation. |
| GO:0043992 histone H3K9 acetyltransferase activity | IDA PMID:29300933 Structural characterization of the Asf1-Rtt109 interaction a... | ACCEPT | Summary: H3K9 acetyltransferase activity by Rtt109 Reason: Direct enzymatic assay confirms H3K9 as Rtt109 substrate. Supporting Evidence: PMID:29300933 Structural characterization of the Asf1-Rtt109 interaction and its role in histone acetylation. |
| GO:0070775 H3 histone acetyltransferase complex | IPI PMID:21256037 Structure of the Rtt109-AcCoA/Vps75 complex and implications... | ACCEPT | Summary: RTT109 is part of H3 histone acetyltransferase complex Reason: RTT109 associates with Vps75 and Asf1 histone chaperones to form active H3 acetyltransferase complexes. Supporting Evidence: PMID:21256037 We report the crystal structure of an Rtt109-AcCoA/Vps75 complex revealing an elongated Vps75 homodimer bound to two globular Rtt109 molecules |
| GO:0032931 histone H3K56 acetyltransferase activity | IDA PMID:18707894 Structural insights into histone H3 lysine 56 acetylation by... | ACCEPT | Summary: H3K56 acetyltransferase activity IDA evidence Reason: Direct biochemical assay of H3K56 acetylation catalyzed by RTT109. Supporting Evidence: PMID:18707894 Structural insights into histone H3 lysine 56 acetylation by Rtt109. |
| GO:0032931 histone H3K56 acetyltransferase activity | IMP PMID:18707894 Structural insights into histone H3 lysine 56 acetylation by... | ACCEPT | Summary: H3K56 acetyltransferase activity IMP evidence Reason: Mutant phenotype: RTT109 mutants unable to acetylate H3K56. Supporting Evidence: PMID:18707894 Structural insights into histone H3 lysine 56 acetylation by Rtt109. |
| GO:0061733 protein-lysine-acetyltransferase activity | IMP PMID:18707894 Structural insights into histone H3 lysine 56 acetylation by... | ACCEPT | Summary: Protein-lysine-acetyltransferase activity demonstrated Reason: Enzymatic characterization confirms lysine acetylation from acetyl-CoA. Supporting Evidence: PMID:18707894 Structural insights into histone H3 lysine 56 acetylation by Rtt109. file:yeast/RTT109/RTT109-deep-research-falcon.md Rtt109 catalyzes **acetyl transfer from acetylβCoA to the Ξ΅βamine of lysine residues on histone H3**, producing acetylβlysine and CoA |
| GO:0005515 protein binding | IPI PMID:31387991 Histone chaperone exploits intrinsic disorder to switch acet... | REMOVE | Summary: The Asf1 interaction is mechanistic but generic protein binding is uninformative. Reason: The Asf1-H3:H4 complex contributes to H3 tail presentation in an Rtt109-Vps75-Asf1 structural model, but GO:0005515 is a generic binding assertion and the review already captures the resulting histone H3 acetyltransferase activities. Supporting Evidence: PMID:31387991 Here, to understand how histone chaperones Asf1 and Vps75 together promote H3 K9-acetylation, we establish the solution structural model of the acetyltransferase Rtt109 in complex with Asf1 and Vps75 and the histone dimer H3:H4. |
| GO:0032931 histone H3K56 acetyltransferase activity | IDA PMID:31387991 Histone chaperone exploits intrinsic disorder to switch acet... | ACCEPT | Summary: Direct Rtt109-Asf1-Vps75 analysis supports H3K56 acetyltransferase activity. Reason: The structural and biochemical study explains how Asf1 and Vps75 tune Rtt109 specificity across the H3 tail and supports retained H3K56 acetyltransferase activity. Supporting Evidence: PMID:31387991 Histone chaperone exploits intrinsic disorder to switch acetylation specificity. |
| GO:0043992 histone H3K9 acetyltransferase activity | IDA PMID:31387991 Histone chaperone exploits intrinsic disorder to switch acet... | ACCEPT | Summary: Rtt109-Vps75 activity toward H3K9 is supported by the chaperone-switching study. Reason: The cited in vitro analysis of Vps75- and Asf1-regulated Rtt109 tail acetylation supports direct H3K9 acetyltransferase activity. Supporting Evidence: PMID:31387991 Histone chaperone exploits intrinsic disorder to switch acetylation specificity. |
| GO:0070775 H3 histone acetyltransferase complex | IDA PMID:31387991 Histone chaperone exploits intrinsic disorder to switch acet... | ACCEPT | Summary: Rtt109 is assayed as an H3 acetyltransferase complex with Vps75 and Asf1. Reason: The paper dissects Rtt109 activity in histone-chaperone complexes, supporting membership in an H3 histone acetyltransferase complex. Supporting Evidence: PMID:31387991 Histone chaperone exploits intrinsic disorder to switch acetylation specificity. |
| GO:0032931 histone H3K56 acetyltransferase activity | IDA PMID:18568037 Fungal Rtt109 histone acetyltransferase is an unexpected str... | ACCEPT | Summary: Direct biochemical and structural evidence supports Rtt109 H3K56 acetyltransferase activity. Reason: The p300/CBP structural-homology study directly characterized fungal Rtt109 as a histone H3 lysine acetyltransferase, including H3K56 activity. Supporting Evidence: PMID:18568037 Fungal Rtt109 histone acetyltransferase is an unexpected structural homolog of metazoan p300/CBP. |
| GO:0032931 histone H3K56 acetyltransferase activity | IMP PMID:18568037 Fungal Rtt109 histone acetyltransferase is an unexpected str... | ACCEPT | Summary: Rtt109 mutant phenotype supports H3K56 acetyltransferase activity in vivo. Reason: The IMP row is consistent with loss of Rtt109-dependent H3K56 acetylation when RTT109 function is perturbed. Supporting Evidence: PMID:18568037 Fungal Rtt109 histone acetyltransferase is an unexpected structural homolog of metazoan p300/CBP. |
| GO:0036408 histone H3K14 acetyltransferase activity | IDA PMID:31194870 Two factor authentication: Asf1 mediates crosstalk between H... | ACCEPT | Summary: Rtt109 acetylates H3K14 through Asf1/Vps75-dependent crosstalk with H3K56 acetylation. Reason: The cited work showed that Asf1 mediates crosstalk between Rtt109 H3K14 and H3K56 acetylation. Supporting Evidence: PMID:31194870 Two factor authentication: Asf1 mediates crosstalk between H3 K14 and K56 acetylation. |
| GO:0043992 histone H3K9 acetyltransferase activity | IDA PMID:31194870 Two factor authentication: Asf1 mediates crosstalk between H... | ACCEPT | Summary: The Asf1/Vps75 crosstalk study supports Rtt109 H3K9 acetyltransferase activity. Reason: The local PMID:31194870 record is abstract-only and names H3K14/H3K56 crosstalk; this residue-specific row defers to SGD's full-text reading and is cross-supported by direct structural and biochemical evidence that Rtt109 acetylates H3K9. Supporting Evidence: PMID:21256037 Yeast Rtt109 promotes nucleosome assembly and genome stability by acetylating K9, K27, and K56 of histone H3 through interaction with either of two distinct histone chaperones, Vps75 or Asf1. |
| GO:0043994 histone H3K23 acetyltransferase activity | IDA PMID:31194870 Two factor authentication: Asf1 mediates crosstalk between H... | ACCEPT | Summary: The Asf1/Vps75 crosstalk study supports Rtt109 H3K23 acetyltransferase activity. Reason: The local PMID:31194870 record is abstract-only and names H3K14/H3K56 crosstalk; this residue-specific row defers to SGD's full-text reading and is cross-supported by direct Rtt109-Vps75 evidence for H3K23 acetylation. Supporting Evidence: PMID:19172748 Acetylation of H3 on K56, K9, K14 and K23 were readily observed as the first set of sites modified |
| GO:0044017 histone H3K27 acetyltransferase activity | IDA PMID:31194870 Two factor authentication: Asf1 mediates crosstalk between H... | ACCEPT | Summary: The Asf1/Vps75 crosstalk study supports Rtt109 H3K27 acetyltransferase activity. Reason: The local PMID:31194870 record is abstract-only and names H3K14/H3K56 crosstalk; this residue-specific row defers to SGD's full-text reading and is cross-supported by direct structural and biochemical evidence that Rtt109 acetylates H3K27. Supporting Evidence: PMID:21256037 Yeast Rtt109 promotes nucleosome assembly and genome stability by acetylating K9, K27, and K56 of histone H3 through interaction with either of two distinct histone chaperones, Vps75 or Asf1. |
| GO:0032931 histone H3K56 acetyltransferase activity | IDA PMID:31194870 Two factor authentication: Asf1 mediates crosstalk between H... | ACCEPT | Summary: The Asf1/Vps75 crosstalk study supports Rtt109 H3K56 acetyltransferase activity. Reason: The paper directly assays how Asf1 and Vps75 tune Rtt109 activity on H3K56 and H3 N-terminal tail lysines. Supporting Evidence: PMID:31194870 Two factor authentication: Asf1 mediates crosstalk between H3 K14 and K56 acetylation. |
| GO:0070775 H3 histone acetyltransferase complex | IDA PMID:31194870 Two factor authentication: Asf1 mediates crosstalk between H... | ACCEPT | Summary: Rtt109 functions in H3 histone acetyltransferase complexes with Asf1 and Vps75. Reason: The Asf1/Vps75 crosstalk paper directly analyzes Rtt109 in chaperone-associated H3 acetyltransferase complexes, so this complex annotation is appropriate. Supporting Evidence: PMID:31194870 Two factor authentication: Asf1 mediates crosstalk between H3 K14 and K56 acetylation. |
| GO:0005515 protein binding | IPI PMID:20560668 Kinetic mechanism of the Rtt109-Vps75 histone acetyltransfer... | REMOVE | Summary: RTT109-Vps75 protein interaction Reason: This row records Rtt109-Vps75 physical association using the generic GO:0005515 term; the specific functional complex and catalytic activities are already captured elsewhere in the review. Supporting Evidence: PMID:20560668 Kinetic mechanism of the Rtt109-Vps75 histone acetyltransferase-chaperone complex. |
| GO:0070775 H3 histone acetyltransferase complex | IDA PMID:20560668 Kinetic mechanism of the Rtt109-Vps75 histone acetyltransfer... | ACCEPT | Summary: Kinetic analysis supports the Rtt109-Vps75 H3 histone acetyltransferase complex. Reason: The cited kinetic work directly characterized the Rtt109-Vps75 acetyltransferase-chaperone complex. Supporting Evidence: PMID:20560668 Kinetic mechanism of the Rtt109-Vps75 histone acetyltransferase-chaperone complex. |
| GO:0005634 nucleus | HDA PMID:14562095 Global analysis of protein localization in budding yeast. | ACCEPT | Summary: High-throughput localization data place Rtt109 in the nucleus. Reason: The genome-wide protein-localization study supports nuclear Rtt109 localization. Supporting Evidence: PMID:14562095 Global analysis of protein localization in budding yeast. |
| GO:1990414 replication-born double-strand break repair via sister chromatid exchange | IMP PMID:23357952 Histone H3K56 acetylation, Rad52, and non-DNA repair factors... | KEEP AS NON CORE | Summary: H3K56 acetylation influences template choice during replication-born double-strand break repair. Reason: The cited genetic study links Rtt109-dependent H3K56 acetylation to repair with the sister chromatid during replication-associated DNA damage. This repair outcome is a downstream consequence of Rtt109-dependent chromatin assembly. Supporting Evidence: PMID:23357952 Histone H3K56 acetylation, Rad52, and non-DNA repair factors control double-strand break repair choice with the sister chromatid. |
| GO:2001032 regulation of double-strand break repair via nonhomologous end joining | IMP PMID:18036332 Interacting proteins Rtt109 and Vps75 affect the efficiency ... | KEEP AS NON CORE | Summary: Rtt109 and Vps75 influence the nonhomologous end-joining branch of double-strand break repair. Reason: The cited study showed that Rtt109 and Vps75 affect nonhomologous end-joining efficiency, supporting this repair-regulation process row as a non-core DNA repair outcome of Rtt109 chromatin activity. Supporting Evidence: PMID:18036332 Interacting proteins Rtt109 and Vps75 affect the efficiency of non-homologous end-joining in Saccharomyces cerevisiae. |
| GO:2001032 regulation of double-strand break repair via nonhomologous end joining | IMP PMID:27222517 Asf1 facilitates dephosphorylation of Rad53 after DNA double... | KEEP AS NON CORE | Summary: Asf1/Rtt109-linked chromatin recovery contributes to double-strand break repair regulation. Reason: The cited mutant phenotypes support a role for the Rtt109-Asf1 pathway in recovery from double-strand breaks and Rad53 dephosphorylation as a non-core outcome of Rtt109-dependent chromatin restoration. Supporting Evidence: PMID:27222517 Asf1 facilitates dephosphorylation of Rad53 after DNA double-strand break repair. |
| GO:0010468 regulation of gene expression | IMP PMID:26941319 Expression homeostasis during DNA replication. | KEEP AS NON CORE | Summary: Rtt109 contributes to gene-expression homeostasis during DNA replication. Reason: Rtt109-dependent H3K56 acetylation helps tune transcription from newly replicated chromatin, supporting this broad regulation-of-gene-expression row as a downstream chromatin effect rather than a core process. Supporting Evidence: PMID:26941319 Expression homeostasis during DNA replication. |
| GO:0005634 nucleus | IDA PMID:15282802 Localization of proteins that are coordinately expressed wit... | ACCEPT | Summary: Cell-cycle localization data place Rtt109 in the nucleus. Reason: The cell-cycle localization study supports a nuclear localization annotation for Rtt109, the compartment where it acetylates nascent histone H3. Supporting Evidence: PMID:15282802 Localization of proteins that are coordinately expressed with Cln2 during the cell cycle. |
| GO:0010484 histone H3 acetyltransferase activity | IMP PMID:17046836 Rtt109 is required for proper H3K56 acetylation: a chromatin... | ACCEPT | Summary: Mutant evidence supports Rtt109 histone H3 acetyltransferase activity. Reason: The H3K56ac study supports the broader H3 acetyltransferase parent term. Supporting Evidence: PMID:17046836 Rtt109 is required for proper H3K56 acetylation: a chromatin mark associated with the elongating RNA polymerase II. |
| GO:0010484 histone H3 acetyltransferase activity | IDA PMID:17272722 Yeast Rtt109 promotes genome stability by acetylating histon... | ACCEPT | Summary: Direct H3K56ac evidence supports the broader H3 acetyltransferase parent term. Reason: This genome-stability study showed Rtt109-dependent acetylation of H3K56, supporting histone H3 acetyltransferase activity. Supporting Evidence: PMID:17272722 Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56. |
| GO:0010484 histone H3 acetyltransferase activity | IMP PMID:17272722 Yeast Rtt109 promotes genome stability by acetylating histon... | ACCEPT | Summary: Genetic H3K56ac evidence supports the broader H3 acetyltransferase parent term. Reason: RTT109 perturbation affects H3K56 acetylation in vivo, which supports histone H3 acetyltransferase activity. Supporting Evidence: PMID:17272722 Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56. |
| GO:0010484 histone H3 acetyltransferase activity | IDA PMID:17272723 Rtt109 acetylates histone H3 lysine 56 and functions in DNA ... | ACCEPT | Summary: Direct evidence for H3K56 acetylation supports Rtt109 H3 acetyltransferase activity. Reason: The cited study demonstrated that Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. Supporting Evidence: PMID:17272723 Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. |
| GO:0010484 histone H3 acetyltransferase activity | IMP PMID:17272723 Rtt109 acetylates histone H3 lysine 56 and functions in DNA ... | ACCEPT | Summary: Mutant evidence for H3K56 acetylation supports Rtt109 H3 acetyltransferase activity. Reason: The IMP row is supported by Rtt109-dependent H3K56 acetylation and DNA replication phenotypes from the same study. Supporting Evidence: PMID:17272723 Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. |
| GO:0010484 histone H3 acetyltransferase activity | IMP PMID:18458063 Chaperone control of the activity and specificity of the his... | ACCEPT | Summary: Chaperone-stimulated activity supports the broad histone H3 acetyltransferase parent term. Reason: The cited biochemical study characterized Rtt109 H3 acetyltransferase activity under histone-chaperone control. Supporting Evidence: PMID:18458063 Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109. |
| GO:0010484 histone H3 acetyltransferase activity | IGI PMID:18458063 Chaperone control of the activity and specificity of the his... | ACCEPT | Summary: Genetic interaction evidence supports the broad histone H3 acetyltransferase parent term. Reason: The IGI row is consistent with the Rtt109 H3 acetyltransferase activity characterized in the same chaperone-control study. Supporting Evidence: PMID:18458063 Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109. |
| GO:0010526 transposable element silencing | IMP PMID:11779788 Multiple regulators of Ty1 transposition in Saccharomyces ce... | ACCEPT | Summary: Rtt109 is required to repress Ty1 retrotransposition. Reason: RTT109 was identified as a regulator of Ty1 transposition, supporting the existing transposable element silencing annotation. Supporting Evidence: PMID:11779788 Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance. |
| GO:0043007 maintenance of rDNA | IGI PMID:23593017 Rtt109 prevents hyper-amplification of ribosomal RNA genes t... | KEEP AS NON CORE | Summary: Rtt109-dependent H3K56 acetylation prevents runaway rDNA copy-number amplification. Reason: The cited study showed that rtt109 mutants hyper-amplify the rDNA array through uncontrolled rolling-circle-type replication. This supports a real locus-specific rDNA-maintenance role downstream of Rtt109 chromatin regulation, but it is secondary to Rtt109's core H3 acetyltransferase activity. Supporting Evidence: PMID:23593017 Rtt109 prevents hyper-amplification of ribosomal RNA genes through histone modification in budding yeast. |
| GO:0004402 histone acetyltransferase activity | EXP PMID:17272722 Yeast Rtt109 promotes genome stability by acetylating histon... | ACCEPT | Summary: Direct H3K56 acetyltransferase evidence also supports the broad histone acetyltransferase parent term. Reason: Rtt109 is experimentally shown to catalyze H3K56 acetylation in an Asf1-stimulated in vitro reaction; GO:0004402 is broad but correct for this direct histone H3 acetyltransferase activity. Supporting Evidence: PMID:17272722 Rtt109p directly catalyzes this modification in vitro in a manner that is stimulated by Asf1p. |
| GO:0004402 histone acetyltransferase activity | EXP PMID:17369253 The Rtt109-Vps75 histone acetyltransferase complex acetylate... | ACCEPT | Summary: The Rtt109-Vps75 complex acetylates non-nucleosomal histone H3. Reason: The cited study purified recombinant and native Rtt109-Vps75 complexes and showed they acetylate free core histone H3, supporting the broad histone acetyltransferase term. Supporting Evidence: PMID:17369253 Rtt109 forms a complex with Vps75 and that both recombinant Rtt109-Vps75 complexes and native complexes purified from yeast cells acetylate H3 present in H3/H4/H2A/H2B core histones but not other histones. |
| GO:0004402 histone acetyltransferase activity | EXP PMID:17690098 Acetylation of lysine 56 of histone H3 catalyzed by RTT109 a... | ACCEPT | Summary: Rtt109 is the catalytic subunit of the Asf1-regulated Rtt109-Vps75 H3K56 acetyltransferase system. Reason: The Rtt109-Vps75 HAT complex catalyzes H3K56 acetylation when Asf1 presents H3/H4 substrate, which supports retaining the broad histone acetyltransferase parent term. Supporting Evidence: PMID:17690098 In budding yeast, acetylation of histone H3 lysine 56 (H3-K56) is catalyzed by the Rtt109-Vps75 histone acetyltransferase (HAT) complex, with Rtt109 being the catalytic subunit |
| GO:0004402 histone acetyltransferase activity | EXP PMID:18568037 Fungal Rtt109 histone acetyltransferase is an unexpected str... | ACCEPT | Summary: Rtt109 is a fungal histone acetyltransferase whose HAT fold and cofactor binding were structurally characterized. Reason: The full-text structural and biochemical study directly analyzed S. cerevisiae Rtt109 bound to acetyl-CoA and established it as an Asf1/Vps75-dependent histone acetyltransferase. Supporting Evidence: PMID:18568037 Rtt109, also known as KAT11, is a recently characterized fungal-specific histone acetyltransferase (HAT) that modifies histone H3 lysine 56 (H3K56) to promote genome stability. |
| GO:0004402 histone acetyltransferase activity | EXP PMID:18707894 Structural insights into histone H3 lysine 56 acetylation by... | ACCEPT | Summary: Rtt109 structures identify the catalytic HAT active site for H3K56 acetylation. Reason: The crystal-structure and biochemical analyses identify the Rtt109 active site, H3K56 anchoring pocket, and K290 autoacetylation site, all supporting histone acetyltransferase activity. Supporting Evidence: PMID:18707894 Using structural and biochemical analyses, we have discovered the catalytic active site and have identified Asp288 as the deprotonation residue and Lys290 as the autoacetylation residue. |
| GO:0004402 histone acetyltransferase activity | EXP PMID:19172748 Molecular functions of the histone acetyltransferase chapero... | ACCEPT | Summary: Vps75 strongly stimulates Rtt109 histone H3 acetyltransferase activity. Reason: This Rtt109-Vps75 biochemical and structural paper supports broad histone acetyltransferase activity by showing chaperone-stimulated H3K56 and H3K9 acetylation. Supporting Evidence: PMID:19172748 We find that Vps75 stimulates the kcat of histone acetylation by approximately 100-fold relative to Rtt109 alone and enhances acetylation of K9 in the H3 histone tail. |
| GO:0004402 histone acetyltransferase activity | EXP PMID:21256037 Structure of the Rtt109-AcCoA/Vps75 complex and implications... | ACCEPT | Summary: The Rtt109-AcCoA/Vps75 holoenzyme mediates H3K9, H3K27 and H3K56 acetylation. Reason: The Rtt109-AcCoA/Vps75 crystal structure and mutational work established Vps75-directed histone H3 acetylation, supporting the broad histone acetyltransferase term. Supporting Evidence: PMID:21256037 Yeast Rtt109 promotes nucleosome assembly and genome stability by acetylating K9, K27, and K56 of histone H3 through interaction with either of two distinct histone chaperones, Vps75 or Asf1. |
| GO:0004402 histone acetyltransferase activity | EXP PMID:29300933 Structural characterization of the Asf1-Rtt109 interaction a... | ACCEPT | Summary: Direct Asf1-Rtt109 interaction contributes to chaperone-dependent histone acetyltransferase activation. Reason: The NMR study explains how the Rtt109 C-terminus engages Asf1 to activate Rtt109 on histone H3 substrate, so the broader HAT parent term is sound. Supporting Evidence: PMID:29300933 Here, we show that in Saccharomyces cerevisiae the Rtt109 C-terminus directly interacts with Asf1 via a surface shared by multiple Asf1 interaction partners |
| GO:0004402 histone acetyltransferase activity | EXP PMID:31194870 Two factor authentication: Asf1 mediates crosstalk between H... | ACCEPT | Summary: Asf1 and Vps75 tune Rtt109 histone acetyltransferase specificity toward H3K14ac-marked H3/H4 substrate. Reason: The chaperone-crosstalk paper biochemically demonstrates Rtt109-Vps75 activity toward histone H3 and shows that Asf1 plus H3K14ac directs H3K56 acetylation. Supporting Evidence: PMID:31194870 We show that pre-acetylated H3K14ac/H4 functions with Asf1 to drive specific acetylation of H3K56 by Rtt109-Vps75. |
| GO:0004402 histone acetyltransferase activity | IEA GO_REF:0000116 | ACCEPT | Summary: RHEA/EC mapping to the general histone acetyltransferase reaction is valid for Rtt109. Reason: Rtt109 is an EC:2.3.1.48 histone acetyltransferase that transfers an acetyl group from acetyl-CoA to histone H3 lysines, so the current RHEA parent activity is a sound automatic assertion. Supporting Evidence: PMID:18719104 Rtt109 is a protein acetyltransferase (PAT) that is responsible for the acetylation of lysine-56 of histone 3 (H3K56) in yeast. |
| GO:0005515 protein binding | IPI PMID:19172749 Histone chaperone specificity in Rtt109 activation. | REMOVE | Summary: The Vps75 interaction is real but generic protein binding is uninformative. Reason: PMID:19172749 supports the specific Rtt109-Vps75 physical and catalytic partnership, but GO:0005515 does not capture the chaperone-stimulated H3 acetyltransferase complex function already represented by accepted complex and catalytic rows. Supporting Evidence: PMID:19172749 Rtt109 forms a complex with the chaperone Vps75 in vivo and is implicated in DNA replication and repair. |
| GO:0005515 protein binding | IPI PMID:31387991 Histone chaperone exploits intrinsic disorder to switch acet... | REMOVE | Summary: The Rtt109-Vps75 interaction is mechanistic but GO:0005515 is too generic. Reason: The structural study uses the Rtt109-Vps75-Asf1 complex to explain H3 tail acetylation specificity; a bare protein-binding row is less informative than the retained H3 histone acetyltransferase complex and lysine-specific H3 acetyltransferase activity annotations. Supporting Evidence: PMID:31387991 Vps75 promotes K9-acetylation by engaging the H3 N-terminal tail in fuzzy electrostatic interactions with its disordered C-terminal domain |
| GO:0061733 protein-lysine-acetyltransferase activity | EXP PMID:18568037 Fungal Rtt109 histone acetyltransferase is an unexpected str... | ACCEPT | Summary: Rtt109 transfers acetyl groups from acetyl-CoA onto histone H3 lysines. Reason: Structure-based mutagenesis plus Rtt109-Vps75 biochemistry support the broader protein-lysine-acetyltransferase parent of Rtt109's histone H3 acetyltransferase activity. Supporting Evidence: PMID:18568037 Rtt109 structure reveals a buried acetylated lysine residue that we show occurs through autoacetylation and that is present in the Rtt109 protein purified from yeast cells. |
| GO:0061733 protein-lysine-acetyltransferase activity | EXP PMID:18719104 Molecular basis for the autoregulation of the protein acetyl... | ACCEPT | Summary: Rtt109 is a protein acetyltransferase with acetyl-CoA bound in its catalytic PAT domain. Reason: The Rtt109-AcCoA structure directly supports the enzyme's acetyl-CoA-dependent lysine acetyltransferase activity and places K290 autoacetylation in its activation mechanism. Supporting Evidence: PMID:18719104 Autoacetylation of lysine-290 within the activation domain is required for stabilizing the interaction between the two domains and is essential for catalysis. |
| GO:0070775 H3 histone acetyltransferase complex | IPI PMID:21256037 Structure of the Rtt109-AcCoA/Vps75 complex and implications... | ACCEPT | Summary: Rtt109 is part of the Vps75-containing H3 histone acetyltransferase complex. Reason: PMID:21256037 structurally characterized the Rtt109-AcCoA/Vps75 holoenzyme and showed that Vps75-Rtt109 contacts are important for the interaction and for H3K9/K27 acetylation, supporting this Vps75-sourced complex row. Supporting Evidence: PMID:21256037 We report the crystal structure of an Rtt109-AcCoA/Vps75 complex revealing an elongated Vps75 homodimer bound to two globular Rtt109 molecules to form a symmetrical holoenzyme |
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Download this section (compressed HTML)Histone acetyltransferase; critical for cell survival in presence of DNA damage during S phase, required for recovery after DSB repair; acetylates H3K56, H3K9; H3K56 acetylation activity required for expression homeostasis, buffering of mRNA synthesis rate against changes in gene dosage during S phase; involved in non-homologous end joining and regulation of Ty1 transposition; prevents hyper-amplification of rDNA; interacts physically with Vps75p
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