Ontology highlight
ABSTRACT:
PROVIDER: PRJNA644463 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR12168534_1.fastq.gz | Fastqsanger.gz | |||
| SRR12168534_2.fastq.gz | Fastqsanger.gz |
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Project description:Tripartite organization of centromeric chromatin in budding yeast
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Project description:Kinetochores are essential macromolecular complexes anchoring chromosomes to the mitotic spindle, ensuring faithful cell division. Despite their critical role, the structural organization of kinetochores over large centromeric regions and across diverse species remains poorly understood. We present the inner kinetochore (CCAN) structure of the silkmoth Bombyx mori, an insect without the canonical centromeric CENP-A gene and with chromosome-wide centromeric activity (holocentric). Our analyses reveal a ring-shaped complex with structural parallels to the known human and yeast kinetochores. Notably, B. mori CCAN incorporates four previously uncharacterized proteins, Centromeric Subunits 1-4, which have unexpected evolutionary relationships to the outer kinetochore Dam1/DASH complex. We demonstrate that CCAN binds DNA as a distinctive head-to-head dimer, folding the DNA into a loop and generating an alternative point-centromere-like architecture poised for chromosome segregation. Our work establishes this self-contained CCAN dimer as a key structural unit that forms the basis of a holocentric organization and suggests that large-scale centromere architectures can emerge from the modular arrangement of such discrete kinetochore units.
2026-04-20 | PXD063391 | Pride
Project description:Drosophila Haspin kinase phosphorylates Histone H3 at threonine 3 at centromeric heterochromatin and either lamin- or polycomb-enriched euchromatic regions, being required for nuclear organization of interphase cells and polycomb-dependent gene silencing.
2020-08-07 | GSE98223 | GEO
Project description:To determine the size and sequence composition of the exceptionally large centromeres in the genome of monocentric Chamaelirium luteum, we performed CENH3-ChIPseq using the customized species-specific CENH3 antibody. We mixed the chromatins of C. luteum and Secale cereal (inbred line Lo7) to dilute the highly abundant centromeric Chama satellite repeats in the C. luteum genome before immunoprecipitation. In addition, H3K4me2- and H3K9me2-ChIPseq were performed to verify the large-scale eu- and heterochromatic genome organization.
2025-11-20 | E-MTAB-16192 | biostudies-arrayexpress
Project description:The biorientation of sister chromatids on the mitotic spindle, essential for accurate sister chromatid segregation, relies on critical centromere components including cohesin, the centromere-specific H3 variant CENP-A, and centromeric DNA. Centromeric DNA is highly variable between chromosomes yet must accomplish a similar function. Moreover, how the 50 nm cohesin ring, proposed to encircle sister chromatids, accommodates inter-sister centromeric distances of hundreds of nanometers on the metaphase spindle is a conundrum. Insight into the 3D organization of centromere components would help resolve how centromeres function on the mitotic spindle. We used ChIP-seq and super-resolution microscopy to examine the geometry of essential centromeric components on human chromosomes. ChIP-seq of SA1, SA2, and Rad21 in human cells demonstrates that cohesin subunits are depleted in -satellite arrays where CENP-A nucleosomes and kinetochores assemble. Cohesin is instead enriched at pericentromeric DNA. Structured illumination microscopy of sister centromeres is consistent, revealing a non-overlapping pattern of CENP-A and cohesin.
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Project description:In eukaryotes, the spatial segregation of heterochromatin and euchromatin is key for the structural organization and function of the genome. Heterochromatin interacts with the nuclear envelope (NE) and occupies a more peripheral position than euchromatin. However, the mechanisms that govern tethering of heterochromatin to the NE are not fully understood. Here, we report that Barrier-to-Autointegration Factor (BAF), a highly conserved NE-associated protein, interacts with centromeric heterochromatin and regulates its anchoring to the NE in a phosphorylation dependent manner. We show that impaired BAF phosphorylation results in its persistent association with centromeric heterochromatin and reinforced anchoring. We also show that reinforced anchoring of centromeric heterochromatin to the NE has important functional consequences, compromising both NE integrity and heterochromatin coalescence, and disturbing mitosis progression and the assembly of functional centromeres. Altogether, our results suggest that anchoring of centromeric heterochromatin to the NE is a highly dynamic process regulated through BAF phosphorylation, and unveil the deleterious functional consequences of perturbing this dynamics.
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Project description:The centromere is a defining feature of eukaryotic chromosomes and is essential for the segregation of chromosomes during cell division. Centromeres are universally marked by the histone variant cenH3 and are restricted to specialized chromatin that most commonly localized to a single position along the chromosome. However, the DNA on which centromeric nucleosomes assemble is not conserved and varies greatly in size and composition. It ranges from genetically defined point centromeres that assemble a single cenH3-containing nucleosome to epigenetically defined regional centromeres embedded in megabases of tandemly repeated DNA to holocentromeres that extend along the length of the entire chromosomes. The organization of regional and holocentric centromeres has so far been elusive, as the precise locations of cenH3-containing sequences could not be determined. Our results show that the point centromere is the basic unit of holocentromeres and provide a basis for understanding how centromeric chromatin is maintained. We use high-resolution mapping of cenH3-associated DNA to show that Caenorhabditids elegans holocentromeres are organized as dispersed but discretely localized point centromeres.
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