ESA1 is a histone acetyltransferase that is essential for growth in yeast

Smith, Edwin R.; Eisen, Arri; Gu, Weigang; Sattah, Martin; Pannuti, Antonio; Zhou, Jianxin; Cook, Richard G.; Lucchesi, John C.; Allis, C. David

doi:10.1073/pnas.95.7.3561

Cited by 286 publications

(311 citation statements)

References 36 publications

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“…Acetylation plays a central role in numerous biological processes, including gene expression [28,29], chromatin dynamics, cell-cycle progression [30][31][32][33], DNA repair [34], and apoptosis. HATs are regulated through various mechanisms, including auto-acetylation, signaling pathways-induced modifications, and cellular metabolites.…”

Section: Hat Function and Regulationsmentioning

confidence: 99%

Acetyltransferases (HATs) as Targets for Neurological Therapeutics

et al. 2013

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The acetylation of histone and non-histone proteins controls a great deal of cellular functions, thereby affecting the entire organism, including the brain. Acetylation modifications are mediated through histone acetyltransferases (HAT) and deacetylases (HDAC), and the balance of these enzymes regulates neuronal homeostasis, maintaining the pre-existing acetyl marks responsible for the global chromatin structure, as well as regulating specific dynamic acetyl marks that respond to changes and facilitate neurons to encode and strengthen longterm events in the brain circuitry (e.g., memory formation). Unfortunately, the dysfunction of these finely-tuned regulations might lead to pathological conditions, and the deregulation of the HAT/HDAC balance has been implicated in neurological disorders. During the last decade, research has focused on HDAC inhibitors that induce a histone hyperacetylated state to compensate acetylation deficits. The use of these inhibitors as a therapeutic option was efficient in several animal models of neurological disorders. The elaboration of new cell-permeant HAT activators opens a new era of research on acetylation regulation. Although pathological animal models have not been tested yet, HAT activator molecules have already proven to be beneficial in ameliorating brain functions associated with learning and memory, and adult neurogenesis in wild-type animals. Thus, HAT activator molecules contribute to an exciting area of research.

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Section: Hat Function and Regulationsmentioning

confidence: 99%

Acetyltransferases (HATs) as Targets for Neurological Therapeutics

et al. 2013

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“…The hypothesis received additional support from the discovery that a mutation within the putative acetyl-CoA-binding motif of Drosophila Mof (male-absent on the first), the fifth protein found to have the MYST domain, compromises its crucial role in gene dosage compensation (Hilfiker et al, 1997). TIP60 and yeast Esa1 (essential Sas2-related acetyltransferase 1) were then demonstrated to possess intrinsic HAT activity (Yamamoto and Horikoshi, 1997;Smith et al, 1998). HBO1 (HAT bound to ORC1) was identified as a binding partner of ORC1 (replication origin complex 1) (Iizuka and Stillman, 1999).…”

Section: Identification Of Moz Morf and Other Mystic Hatsmentioning

confidence: 99%

MOZ and MORF, two large MYSTic HATs in normal and cancer stem cells

2007

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Genes of the human monocytic leukemia zinc-finger protein MOZ (HUGO symbol, MYST3) and its paralog MORF (MYST4) are rearranged in chromosome translocations associated with acute myeloid leukemia and/or benign uterine leiomyomata. Both proteins have intrinsic histone acetyltransferase activity and are components of quartet complexes with noncatalytic subunits containing the bromodomain, plant homeodomain-linked (PHD) finger and proline-tryptophan-tryptophan-proline (PWWP)-containing domain, three types of structural modules characteristic of chromatin regulators. Although leukemia-derived fusion proteins such as MOZ-TIF2 promote self-renewal of leukemic stem cells, recent studies indicate that murine MOZ and MORF are important for proper development of hematopoietic and neurogenic progenitors, respectively, thereby highlighting the importance of epigenetic integrity in safeguarding stem cell identity.

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“…This observation raises the possibility that some other component of the SAGA complex is a critical mediator of Mycdependent gene regulation. One possibility is that TRRAP is associated with another histone acetyltransferase such as the mammalian ortholog of the essential ESA1p protein (called TIP60 in humans) (Kamine et al, 1996;Smith et al, 1998b). However, preliminary experiments fail to show an interaction between Myc and TIP60 (S McMahon, unpublished results).…”

Section: Trrap Links Myc Transactivation To Chromatin Remodeling and mentioning

confidence: 99%