SAS-mediated acetylation of histone H4 Lys 16 is required for H2A.Z incorporation at subtelomeric regions in <i>Saccharomyces cerevisiae</i>

Shia, Wei Jong; Li, Bing; Workman, Jerry L.

doi:10.1101/gad.1439206

Cited by 94 publications

(101 citation statements)

References 39 publications

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“…With respect to histone variants, studies in yeast have shown that H4K16 acetylation is a prerequisite to the incorporation of Htz1 Shia et al, 2006), the counterpart of the mammalian H2A.Z, an H2A variant involved in transcription activation and implicated in maintaining the boundaries of heterochromatin in yeast. Also, deacetylation of K16 is directly linked to histone H1 isoform H1.4 recruitment in mammalian cells upon silencing (Vaquero et al, 2004).…”

Section: Histone H4 Lysine 16 Interplaysmentioning

confidence: 99%

NAD+-dependent deacetylation of H4 lysine 16 by class III HDACs

2007

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Histone deacetylases (HDACs) catalyse the removal of acetyl groups from the N-terminal tails of histones. All known HDACs can be categorized into one of four classes (I-IV). The class III HDAC or silencing information regulator 2 (Sir2) family exhibits characteristics consistent with a distinctive role in regulation of chromatin structure. Accumulating data suggest that these deacetylases acquired new roles as genomic complexity increased, including deacetylation of non-histone proteins and functional diversification in mammals. However, the intrinsic regulation of chromatin structure in species as diverse as yeast and humans, underscores the pressure to conserve core functions of class III HDACs, which are also known as Sirtuins. One of the key factors that might have contributed to this preservation is the intimate relationship between some members of this group of proteins (SirT1, SirT2 and SirT3) and deacetylation of a specific residue in histone H4, lysine 16 (H4K16). Evidence accumulated over the years has uncovered a unique role for H4K16 in chromatin structure throughout eukaryotes. Here, we review the recent findings about the functional relationship between H4K16 and the Sir2 class of deacetylases and how that relationship might impact aging and diseases including cancer and diabetes.

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Section: Histone H4 Lysine 16 Interplaysmentioning

confidence: 99%

NAD+-dependent deacetylation of H4 lysine 16 by class III HDACs

2007

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“…However, Sas2's telomeric silencing function stems from its role as a boundary factor in preventing the spreading of heterochromatin into euchromatic regions (Kimura et al, 2002;Suka et al, 2002), rather than from direct promoter acetylation. In addition, the boundary function of Sas2 may entail the deposition of H2A.Z in subtelomeric regions (Shia et al, 2006). Therefore, by analogy, dTip60 may also act in gene repression in flies as a boundary factor by restricting heterochromatin to its designated genomic region.…”

Section: Dtip60 Might Mediate Its Repressive Function By Deposition Omentioning

confidence: 99%

Widespread regulation of gene expression in the Drosophila genome by the histone acetyltransferase dTip60

et al. 2009

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“…SAS-I globally acetylates H4 K16 in subtelomeric regions (17). Similarly, the HDAC Rpd3 provides global chromatin deacetylation in addition to its function in local gene repression (18).…”

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confidence: 99%

Rpd3-dependent boundary formation at telomeres by removal of Sir2 substrate

Ehrentraut

Weber

Dybowski

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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Boundaries between euchromatic and heterochromatic regions until now have been associated with chromatin-opening activities. Here, we identified an unexpected role for histone deacetylation in this process. Significantly, the histone deacetylase (HDAC) Rpd3 was necessary for boundary formation in Saccharomyces cerevisiae . rpd3 Δ led to silent information regulator (SIR) spreading and repression of subtelomeric genes. In the absence of a known boundary factor, the histone acetyltransferase complex SAS-I, rpd3 Δ caused inappropriate SIR spreading that was lethal to yeast cells. Notably, Rpd3 was capable of creating a boundary when targeted to heterochromatin. Our data suggest a mechanism for boundary formation whereby histone deacetylation by Rpd3 removes the substrate for the HDAC Sir2, so that Sir2 no longer can produce O-acetyl-ADP ribose (OAADPR) by consumption of NAD + in the deacetylation reaction. In essence, OAADPR therefore is unavailable for binding to Sir3, preventing SIR propagation.

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SAS-mediated acetylation of histone H4 Lys 16 is required for H2A.Z incorporation at subtelomeric regions in Saccharomyces cerevisiae

Cited by 94 publications

References 39 publications

NAD+-dependent deacetylation of H4 lysine 16 by class III HDACs

NAD+-dependent deacetylation of H4 lysine 16 by class III HDACs

Widespread regulation of gene expression in the Drosophila genome by the histone acetyltransferase dTip60

Rpd3-dependent boundary formation at telomeres by removal of Sir2 substrate

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