Nuclear Envelope Proteins Modulating the Heterochromatin Formation and Functions in Fission Yeast

Hirano, Yasuhiro; Asakawa, Haruhiko; Sakuno, Takeshi; Haraguchi, Tokuko; Hiraoka, Yasushi

doi:10.3390/cells9081908

Cited by 15 publications

(15 citation statements)

References 165 publications

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“…The nuclear envelope (NE) remains intact throughout the cell cycle (closed mitosis) unlike higher animals and plants, in which the NE disassembles during mitosis (open mitosis). In the mitotic interphase, centromeres are associated with the spindle-pole body (SPB, a centrosome-equivalent structure in fungi), and telomeres are on the NE at the opposite side of SPB (reviewed in [ 7 ]). Telomeres are anchored to the NE through interaction between telomere protein Rap1, a component of shelterin, and NE protein Bqt4 [ 8 , 9 ].…”

Section: Nuclear Organization In S Pombementioning

confidence: 99%

Subtelomeric Chromatin in the Fission Yeast S. pombe

et al. 2021

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Telomeres play important roles in safeguarding the genome. The specialized repressive chromatin that assembles at telomeres and subtelomeric domains is key to this protective role. However, in many organisms, the repetitive nature of telomeric and subtelomeric sequences has hindered research efforts. The fission yeast S. pombe has provided an important model system for dissection of chromatin biology due to the relative ease of genetic manipulation and strong conservation of important regulatory proteins with higher eukaryotes. Telomeres and the telomere-binding shelterin complex are highly conserved with mammals, as is the assembly of constitutive heterochromatin at subtelomeres. In this review, we seek to summarize recent work detailing the assembly of distinct chromatin structures within subtelomeric domains in fission yeast. These include the heterochromatic SH subtelomeric domains, the telomere-associated sequences (TAS), and ST chromatin domains that assemble highly condensed chromatin clusters called knobs. Specifically, we review new insights into the sequence of subtelomeric domains, the distinct types of chromatin that assemble on these sequences and how histone H3 K36 modifications influence these chromatin structures. We address the interplay between the subdomains of chromatin structure and how subtelomeric chromatin is influenced by both the telomere-bound shelterin complexes and by euchromatic chromatin regulators internal to the subtelomeric domain. Finally, we demonstrate that telomere clustering, which is mediated via the condensed ST chromatin knob domains, does not depend on knob assembly within these domains but on Set2, which mediates H3K36 methylation.

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Section: Nuclear Organization In S Pombementioning

confidence: 99%

Subtelomeric Chromatin in the Fission Yeast S. pombe

et al. 2021

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“…Heterochromatin assembly is strictly regulated for accurate chromosome segregation, maintenance of telomere integrity, transcriptional silencing, and transposon control [ 112 , 114 ]. S. pombe is an excellent study model to discern and understand the epigenetic mechanism regulating heterochromatin assembly [ 21 ]. Furthermore, S. pombe ’s genome presents a single copy of the genes encoding RNAi proteins: Argonaute (Ago1), Dicer (Dcr1), and RNA-dependent RNA polymerase (Rdp1) [ 53 , 115 ].…”

Section: Heterochromatin Formationmentioning

confidence: 99%

“…These proteins form a multiprotein complex located at the perinuclear region that acts generating MSUD-associated siRNAs (masiRNAs) [ 20 ]. After these first discoveries in N. crassa , the RNAi mechanism was found in several other fungi, such as Schizosaccharomyces pombe [ 21 ], Cryptococcus [ 22 ], or Mucor [ 23 ].…”

Section: Introductionmentioning

confidence: 99%

The Evolutionary Significance of RNAi in the Fungal Kingdom

Lax

Tahiri

Patiño-Medina

et al. 2020

IJMS

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RNA interference (RNAi) was discovered at the end of last millennium, changing the way scientists understood regulation of gene expression. Within the following two decades, a variety of different RNAi mechanisms were found in eukaryotes, reflecting the evolutive diversity that RNAi entails. The essential silencing mechanism consists of an RNase III enzyme called Dicer that cleaves double-stranded RNA (dsRNA) generating small interfering RNAs (siRNAs), a hallmark of RNAi. These siRNAs are loaded into the RNA-induced silencing complex (RISC) triggering the cleavage of complementary messenger RNAs by the Argonaute protein, the main component of the complex. Consequently, the expression of target genes is silenced. This mechanism has been thoroughly studied in fungi due to their proximity to the animal phylum and the conservation of the RNAi mechanism from lower to higher eukaryotes. However, the role and even the presence of RNAi differ across the fungal kingdom, as it has evolved adapting to the particularities and needs of each species. Fungi have exploited RNAi to regulate a variety of cell activities as different as defense against exogenous and potentially harmful DNA, genome integrity, development, drug tolerance, or virulence. This pathway has offered versatility to fungi through evolution, favoring the enormous diversity this kingdom comprises.

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“…So far, mammalian lamin orthologs have not been detected in yeasts, either experimentally [30] or in silico [25]. However, in spite of lacking canonical lamins, yeast NPC components, nucleoporins and NEassociated proteins provide a platform for anchoring chromatin to the NE and for events related to gene expression regulation, transcription, mitosis and NE stability [31][32][33]. Lamins are likely the ancestral lamina proteins while the more restricted plant and kinetoplastid systems appear to be lineage specific and likely later emerging [25].…”

Section: Introductionmentioning

confidence: 99%

Evolution and diversification of the nuclear envelope

Padilla-Mejía

Макаров

Barlow

et al. 2021

Nucleus

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Eukaryotic cells arose ~1.5 billion years ago, with the endomembrane system a central feature, facilitating evolution of intracellular compartments. Endomembranes include the nuclear envelope (NE) dividing the cytoplasm and nucleoplasm. The NE possesses universal features: a double lipid bilayer membrane, nuclear pore complexes (NPCs), and continuity with the endoplasmic reticulum, indicating common evolutionary origin. However, levels of specialization between lineages remains unclear, despite distinct mechanisms underpinning various nuclear activities. Several distinct modes of molecular evolution facilitate organellar diversification and to understand which apply to the NE, we exploited proteomic datasets of purified nuclear envelopes from model systems for comparative analysis. We find enrichment of core nuclear functions amongst the widely conserved proteins to be less numerous than lineage-specific cohorts, but enriched in core nuclear functions. This, together with consideration of additional evidence, suggests that, despite a common origin, the NE has evolved as a highly diverse organelle with significant lineage-specific functionality.

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Nuclear Envelope Proteins Modulating the Heterochromatin Formation and Functions in Fission Yeast

Cited by 15 publications

References 165 publications

Subtelomeric Chromatin in the Fission Yeast S. pombe

Subtelomeric Chromatin in the Fission Yeast S. pombe

The Evolutionary Significance of RNAi in the Fungal Kingdom

Evolution and diversification of the nuclear envelope

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