RTT109 Antibody

1. This replication-guided H3K9ac was fully dependent on the acetyltransferase Rtt109, while expression-guided H3K9ac was deposited by Gcn5. Further, topoisomerase depletion intensified H3K9ac in front of the replication fork and in sites where RNA polymerase II was trapped, suggesting supercoiling stresses trigger H3K9 acetylation. PMID: 27225843
2. The absence of RTT109 enhanced resistance to 5.5 g L(-1) acetic acid, which was indicated by improved growth of RTT109Delta mutant compared with that of the wild-type BY4741 strain. PMID: 26851403
3. Vps75 and Asf1 both enhance Rtt109 acetylation for H3/H4 PMID: 25781956
4. Lys290 in Rtt109 is required in vivo for Vps75 to enhance the activity of the histone acetyltransferase. PMID: 23457193
5. Rtt109-Vps75 preferentially acetylates H3 K9 and K23 PMID: 23036725
6. We propose that, in the rtt109 mutant, rDNA hyper-amplification is caused by uncontrolled rolling-circle-type replication PMID: 23593017
7. Findings suggest that functional switching of Asf1 between states that close and open chromatin is under physiological control by a pathway that depends on Rtt109. PMID: 22106264
8. Autoacetylation of the histone acetyltransferase Rtt109. PMID: 21606491
9. Data show that Rtt109 nuclear localization depends on Vps75, and nuclear localization of the Vps75-Rtt109 complex is not critical for Rtt109-dependent functions. PMID: 21463458
10. Histone chaperones, Vps75 or Asf1, dictate Histone acetyltransferase, Rtt109, substrate specificity through distinct mechanisms. PMID: 21256037
11. the basis for the enhanced acetylation of histone H3 tail residues by Vps75-Rtt109. PMID: 21454705
12. Data provide the framework for a postreplicative recombination mechanism controlled by histone modifiers Rtt109 and histone chaperones Cia1/Asf1 in multiple ways. PMID: 20718939
13. Rtt109 variants with interface point substitutions lack the ability to be fully activated by Vps75, and one such variant displayed impaired Vps75-dependent histone acetylation function. PMID: 21057107
14. Rtt109p regulates the deposition/eviction of histone H2B in addition to its role in stimulating histone H3 eviction, thus providing insight into chromatin assembly/disassembly and hence gene expression in vivo. PMID: 20668333
15. Rtt109 and H3K56 acetylation appear to correlate with actively transcribed genes and associate with the elongating form of polymerase II PMID: 17046836
16. data establish Rtt109p as a member of a new class of histone acetyltransferases and show that its actions are critical for cell survival in the presence of DNA damage during S phase PMID: 17272722
17. findings show that Rtt109 is a histone H3 lysine 56 histone acetyltransferase; it shares no sequence homology with any other known HATs PMID: 17272723
18. These results indicate that Rtt109, Rtt101, and Rtt107, which genetic evidence suggests are functionally related, form a DNA damage response pathway that recruits Rtt107 complexes to damaged or stalled replication forks. PMID: 17978089
19. one function of the Rtt109-Vps75 interacting protein pair is to affect the efficiency of NHEJ in yeast PMID: 18036332
20. Acetylation of Saccharomyces cerevisiae histone H3 on K56 by the histone acetyltransferase (HAT) Rtt109 is important for repairing replication-associated lesions. PMID: 18458063
21. The Rtt109 structure reveals noteworthy homology to the metazoan p300/CBP HAT domain but exhibits functional divergence, including atypical catalytic properties and mode of cofactor regulation. PMID: 18568037
22. Structural insights to understand the acetylation mechanism of H3-K56 by Rtt109. PMID: 18707894
23. autoacetylation of Rtt109 is crucial for the regulation of its catalytic activity PMID: 18719104
24. two surfaces on the earmuff domain of Vps75 participate in Rtt109 interaction with a stoichiometry of 2:1 PMID: 18723682
25. Histone H3 lysine 56 acetylation by Rtt109 is crucial for chromosome positioning PMID: 19001125
26. probed the molecular functions of Vps75 and the Rtt109-Vps75 complex through biochemical, structural and genetic means PMID: 19172748
27. both Rtt109 and Vps75 bind histones with high affinity, but only the complex is efficient for catalysis PMID: 19172749
28. Results indicate a role for Vps75 in nucleosome dynamics during transcription, and importantly, this function appears to be largely independent of Rtt109. PMID: 19470761

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KEGG: sce:YLL002W

STRING: 4932.YLL002W