The interplay of histone H2B ubiquitination with budding and fission yeast heterochromatin

Zukowski, Alexis; Johnson, Aaron

doi:10.1007/s00294-018-0812-1

Cited by 9 publications

(2 citation statements)

References 69 publications

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“…The ubiquitination of H2BK123 in budding yeast, mediated by Rad6 and Bre1, is often a prerequisite for the establishment of other histone PTMs, including H3K4me and H3K79me [106,107,108,109]. It is also reported to have a role in replicative lifespan regulation through interaction with the Sir2 pathway [110].…”

Section: Histone Modifications and Chromatin Dynamicsmentioning

confidence: 99%

Histone Modifications and the Maintenance of Telomere Integrity

Jezek¹,

Green²

2019

Cells

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Telomeres, the nucleoprotein structures at the ends of eukaryotic chromosomes, play an integral role in protecting linear DNA from degradation. Dysregulation of telomeres can result in genomic instability and has been implicated in increased rates of cellular senescence and many diseases, including cancer. The integrity of telomeres is maintained by a coordinated network of proteins and RNAs, such as the telomerase holoenzyme and protective proteins that prevent the recognition of the telomere ends as a DNA double-strand breaks. The structure of chromatin at telomeres and within adjacent subtelomeres has been implicated in telomere maintenance pathways in model systems and humans. Specific post-translational modifications of histones, including methylation, acetylation, and ubiquitination, have been shown to be necessary for maintaining a chromatin environment that promotes telomere integrity. Here we review the current knowledge regarding the role of histone modifications in maintaining telomeric and subtelomeric chromatin, discuss the implications of histone modification marks as they relate to human disease, and highlight key areas for future research.

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Section: Histone Modifications and Chromatin Dynamicsmentioning

confidence: 99%

Histone Modifications and the Maintenance of Telomere Integrity

Jezek¹,

Green²

2019

Cells

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“…Hence, even in systems such as mammals where DNA methylation is thought to support H3K9 methylation, the stability of distal heterochromatin requires the non-enzymatic subunits of the spreading enzyme complex, including methyl histone reader proteins [28], to be present continuously. Antagonizing activities [29][30][31] have been shown to be able to encroach on heterochromatin [32], pointing to the involvement of dynamic forces in shaping and mainiting the epigneome beyond replication. Hence, "copying" of heterochromatin is not sufficient to maintain the epigenetic pattern.…”

Section: B Mechanisms Of Distal Heterochromatin Epigenetic Inheritancementioning

confidence: 99%

Epigenetic fates of gene silencing established by heterochromatin spreading in cell identity and genome stability

Greenstein

Al-Sady

2018

Curr Genet

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Heterochromatin spreading, the propagation of repressive chromatin along the chromosome, is a reaction critical to genome stability and defense, as well as maintenance of unique cell fates. Here, we discuss the intrinsic properties of the spreading reaction and circumstances under which its products, formed distal to DNA-encoded nucleation sites, can be epigenetically maintained. Finally, we speculate that the epigenetic properties of heterochromatin evolved together with the need to stabilize cellular identity.

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How does Hsp90 function in RNAi-dependent heterochromatin assembly?

2018

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Heat-shock protein 90 (Hsp90) was recently identified as a silencing factor required for RNA interference (RNAi)-dependent heterochromatin assembly in the fission yeast Schizosaccharomyces pombe. As Hsp90 is known to contribute to the formation of small RNA-containing effector complexes, it would be expected that Hsp90 is also involved in the RNAi pathway in fission yeast. However, upon investigation, we found it very difficult to determine how Hsp90 modulates RNAi-dependent heterochromatin assembly in the cell. A lack of detectable small interfering RNAs in hsp90 mutant cells prevented us from examining the role of Hsp90 in the siRNA loading in the cell. In addition, deletion of genes encoding co-chaperones for Hsp90 appears not to affect RNAi-dependent pericentromeric silencing. One possible approach for elucidating the role of Hsp90 in RNAi-dependent heterochromatin assembly is the use of forward genetic screens to identify novel factors linking Hsp90 with other known RNAi factors. Here, we discuss the benefits of conducting further screenings and present some technical hints to help identify new factors.

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The interplay of histone H2B ubiquitination with budding and fission yeast heterochromatin

Cited by 9 publications

References 69 publications

Histone Modifications and the Maintenance of Telomere Integrity

Histone Modifications and the Maintenance of Telomere Integrity

Epigenetic fates of gene silencing established by heterochromatin spreading in cell identity and genome stability

How does Hsp90 function in RNAi-dependent heterochromatin assembly?

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