Transcriptional silencing in fission yeast

Grewal, Shiv I. S.

doi:10.1002/1097-4652(200009)184:3<311::aid-jcp4>3.0.co;2-d

Cited by 76 publications

(46 citation statements)

References 78 publications

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“…A second motif which has been shown to bind modified histones is the chromodomain, which preferentially interacts with methylated lysines (19,52). Chromodomains are found in proteins involved in both the activation and silencing of transcription, consistent with the role of histone methylation in both events (31).…”

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confidence: 94%

The Yng1p Plant Homeodomain Finger Is a Methyl-Histone Binding Module That Recognizes Lysine 4-Methylated Histone H3

Martin¹,

Baetz

Shi

et al. 2006

Molecular and Cellular Biology

145

114

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The ING (inhibitor of growth) protein family includes a group of homologous nuclear proteins that share a highly conserved plant homeodomain (PHD) finger domain at their carboxyl termini. Members of this family are found in multiprotein complexes that posttranslationally modify histones, suggesting that these proteins serve a general role in permitting various enzymatic activities to interact with nucleosomes. There are three members of the ING family in Saccharomyces cerevisiae: Yng1p, Yng2p, and Pho23p. Yng1p is a component of the NuA3 histone acetyltransferase complex and is required for the interaction of NuA3 with chromatin. To gain insight into the function of the ING proteins, we made use of a genetic strategy to identify genes required for the binding of Yng1p to histones. Using the toxicity of YNG1 overexpression as a tool, we showed that Yng1p interacts with the amino-terminal tail of histone H3 and that this interaction can be disrupted by loss of lysine 4 methylation within this tail. Additionally, we mapped the region of Yng1p required for overexpression of toxicity to the PHD finger, showed that this region capable of binding lysine 4-methylated histone H3 in vitro, and demonstrated that mutations of the PHD finger that abolish binding in vitro are no longer toxic in vivo. These results identify a novel function for the Yng1p PHD finger in promoting stabilization of the NuA3 complex at chromatin through recognition of histone H3 lysine 4 methylation.Chromatin structure can be regulated by the addition of posttranslational modifications to histones, including acetylation, methylation, phosphorylation, and ubiquitination. These modifications are thought to function by creating docking sites for factors which alter chromatin structure (27,58). Consistent with this, several protein motifs have been identified that mediate the selective interaction of transcription-regulating complexes with specific histone modifications. The first such identified motif is the bromodomain, which preferentially interacts with acetylated histones (7,10,24,49,50,65). Bromodomains are found in a number of protein complexes, including components of the basal transcription machinery and chromatin remodeling complexes (20, 41), which may explain, in part, how histone acetylation can facilitate transcription. Bromodomains are also found in a number of histone methyltransferases, suggesting that histone acetylation can mediate histone methylation (6). The ability of one histone modification to recruit another histone-modifying enzyme is a common recurring theme in chromatin research.A second motif which has been shown to bind modified histones is the chromodomain, which preferentially interacts with methylated lysines (19,52). Chromodomains are found in proteins involved in both the activation and silencing of transcription, consistent with the role of histone methylation in both events (31). Similar to bromodomains, chromodomains are found in chromatin remodeling complexes, histone acetyltransferases, and histone methyltransfer...

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mentioning

confidence: 94%

The Yng1p Plant Homeodomain Finger Is a Methyl-Histone Binding Module That Recognizes Lysine 4-Methylated Histone H3

Martin¹,

Baetz

Shi

et al. 2006

Molecular and Cellular Biology

145

114

View full text Add to dashboard Cite

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“…T HE assembly of heterochromatin domains along eukaryotic chromosomes is essential for several chromosomal functions, including proper chromosome segregation, inhibition of deleterious recombination, and dosage compensation (reviewed in Allshire 1997; Karpen and Allshire 1997;Grewal 2000;Martin and Zhang 2005;Zardo et al 2005). However, unrestricted spreading of heterochromatin is detrimental, as it may repress expression of essential genes and tumor-suppressor genes.…”

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confidence: 99%

Interaction of Epe1 With the Heterochromatin Assembly Pathway inSchizosaccharomyces pombe

et al. 2007

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Epe1 is a JmjC domain protein that antagonizes heterochromatization in Schizosaccharomyces pombe. Related JmjC domain proteins catalyze a histone demethylation reaction that depends on Fe(II) and a-ketoglutarate. However, no detectable demethylase activity is associated with Epe1, and its JmjC domain lacks conservation of Fe(II)-binding residues. We report that Swi6 recruits Epe1 to heterochromatin and that overexpression of epe1 1 , like mutations in silencing genes or overexpression of swi6 1 , upregulates expression of certain genes. A significant overlap was observed between the lists of genes that are upregulated by overexpression of epe1 1 and those that are upregulated by mutations in histone deacetylase genes. However, most of the common genes are not regulated by Clr4 histone methyltransferase. This suggests that Epe1 interacts with the heterochromatin assembly pathway at the stage of histone deacetylation. Mutational inactivation of Epe1 downregulates $12% of S. pombe genes, and the list of these genes overlaps significantly with the lists of genes that are upregulated by mutations in silencing genes and genes that are hyperacetylated at their promoter regions in clr6-1 mutants. We propose that an interplay between the repressive HDACs activity and Epe1 helps to regulate gene expression in S. pombe.

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“…These studies abdominal-A (abd-A), and Abdominal-B (Abd-B), which specdemonstrate that domains correspond to units of indeify segment identity in the posterior parasegments (PS) pendent genetic activity, and that each domain has its 5-14 of the fly. The parasegment-specific expression of own distinct nucleoprotein composition and chromatin these three homeotic genes is controlled by an ‫-003ف‬ structure depending upon the developmental stage, tiskb cis-regulatory region that is subdivided into nine parasue, or cell type and whether the domain is active or segment-specific cis-regulatory domains: abx/bx, bxd/pbx, inactive (Kellum and Elgin 1998;Gerasimova and and iab2-9 (Lewis 1978;Sanchez-Herrero et al 1985;Corces 1999;Udvardy 1999;Grewal 2000;West et Karch et al 1985;Casanova and White 1987;Duncan al. 2002).…”

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The Enhancer-Blocking Activity of the Fab-7 Boundary From the Drosophila Bithorax Complex Requires GAGA-Factor-Binding Sites

et al. 2004

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In the work reported here we have analyzed the role of the GAGA factor [encoded by the Trithorax-like (Trl) gene] in the enhancer-blocking activity of Frontabdominal-7 (Fab-7), a domain boundary element from the Drosophila melanogaster bithorax complex (BX-C). One of the three nuclease hypersensitive sites in the Fab-7 boundary, HS1, contains multiple consensus-binding sequences for the GAGA factor, a protein known to be involved in the formation and/or maintenance of nucleosome-free regions of chromatin. GAGA protein has been shown to localize to the Fab-7 boundary in vivo, and we show that it recognizes sequences from HS1 in vitro. Using two different transgene assays we demonstrate that GAGA-factor-binding sites are necessary but not sufficient for full Fab-7 enhancer-blocking activity. We show that distinct GAGA sites are required for different enhancer-blocking activities at different stages of development. We also show that the enhancer-blocking activity of the endogenous Fab-7 boundary is sensitive to mutations in the gene encoding the GAGA factor Trithorax-like.

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Transcriptional silencing in fission yeast

Cited by 76 publications

References 78 publications

The Yng1p Plant Homeodomain Finger Is a Methyl-Histone Binding Module That Recognizes Lysine 4-Methylated Histone H3

The Yng1p Plant Homeodomain Finger Is a Methyl-Histone Binding Module That Recognizes Lysine 4-Methylated Histone H3

Interaction of Epe1 With the Heterochromatin Assembly Pathway inSchizosaccharomyces pombe

The Enhancer-Blocking Activity of the Fab-7 Boundary From the Drosophila Bithorax Complex Requires GAGA-Factor-Binding Sites

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