ESA1 Antibody

1. NuA4 acetylates Htz1 Lys 14 (K14) after the histone is assembled into chromatin by the SWR-C. K14 mutants exhibit specific defects in chromosome transmission without affecting transcription, telomeric silencing, or DNA repair [NuA4] PMID: 16543219
2. urther our work suggests that NuA4 regulates acetyl-CoA levels through the Acetyl-CoA carboxylase Acc1. Altogether this work establishes both NuA4 and the metabolite acetyl-CoA as critical signaling pathways regulating the formation of glucose-deprived stress granules. PMID: 28231279
3. Deletion of HOS2 modulated the transcriptional response of ESA1 cells upon DNA damage. PMID: 26303527
4. In the absence of NuA4, ribosomal protein genes lose TFIID dependency and become SAGA dependent for transcriptional initiation. PMID: 26100014
5. Data indicate that histine acetyltransferase NuA4 interaction with nucleosomes is stimulated by histne lysines H3K4 and H3K36 methylation. PMID: 25301943
6. Esa1 Tudor domain loop region is positioned close to nucleosomal DNA PMID: 23109429
7. Evidence that Nab3 is a nonhistone substrate of Esa1 whose function may be influenced by acetylation. PMID: 23050233
8. identified Esa1 as a histone acetyltransferase required for autophagy; identified Atg3 as a substrate for Esa1; acetylation of K19 and K48 of Atg3 regulated autophagy by controlling Atg3 and Atg8 interaction and lipidation of Atg8 PMID: 22539722
9. homocitrate synthase encoded by LYS20 in yeast is linked to the key process of DNA damage repair through the essential MYST family histone acetyltransferase Esa1 and the H2A.Z histone variant PMID: 20810648
10. A model whereby Esa1 and Rpd3L act coordinately to control the acetylation of H4 lysine 12 to regulate transcription and dynamic acetylation and deacetylation of this particular histone residue and maintain cell viability. PMID: 19596907
11. A functional analysis was made of the ESA1-containing Piccolo NuA4 histone acetyltransferase complex. PMID: 15964809
12. Esa1p also plays a key role in silencing RNA polymerase II (Pol II)-transcribed genes at telomeres and within the ribosomal DNA (rDNA) of the nucleolus. PMID: 16436512
13. steady-state kinetic analyses revealed a kinetic mechanism that requires the formation of a ternary complex prior to catalysis, where acetyl-CoA binds first and CoA is the last product released PMID: 17223684
14. The essential function of Esa1 may be to bind acetyl-CoA or lysine substrates and positively regulate the activities of NuA4 and Piccolo NuA4. PMID: 18245364
15. Results describe how the novel structure of the knotted tudor domain of Esa1 impacts on RNA binding and how this influences in vivo function. PMID: 18407291

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KEGG: sce:YOR244W

STRING: 4932.YOR244W