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Centromeric chromatin in mitosis reorganizes into a functional structure stabilized by cohesin [CENPA-ChIP-seq]

ABSTRACT: Centromeric chromatin in mitosis reorganizes into a functional structure stabilized by cohesin [CENPA-ChIP-seq]

PROVIDER: PRJNA1068948 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR27723072_1.fastq.gz	Fastqsanger.gz
	SRR27723072_2.fastq.gz	Fastqsanger.gz
	SRR27723073_1.fastq.gz	Fastqsanger.gz
	SRR27723073_2.fastq.gz	Fastqsanger.gz
	SRR27723074.fastq.gz	Fastqsanger.gz

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Centromeric chromatin in mitosis reorganizes into a functional structure stabilized by cohesin

Project description:Centromeric chromatin in mitosis reorganizes into a functional structure stabilized by cohesin

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Centromeric chromatin in mitosis reorganizes into a functional structure stabilized by cohesin [Halo-ChIP-seq]

Project description:Centromeric chromatin in mitosis reorganizes into a functional structure stabilized by cohesin [Halo-ChIP-seq]

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Centromeric chromatin in mitosis reorganizes into a functional structure stabilized by cohesin [NG-Capture-C]

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CENPA as a reader of m6A-modified centromeric RNA to ensure centromere integrity in cancer cells [CHIP-seq]

Project description:Maintaining centromere integrity is crucial for genome stability and proper chromosome segregation during mitosis. CENPA, a conserved histone H3 variant, is localized at the centromeres and plays an essential role in preserving centromere integrity and function. However, the mechanisms that retain CENPA at centromeres remain an enigma. In this study, we identified CENPA as an m6A reader of centromeric RNA (cenRNA), which is essential for its centromeric localization and function in maintaining centromere stability. We discovered a higher level of m6A modification on cenRNA in cancerous cells compared to normal cells. CENPA preferentially binds the cenRNAs with m6A modification, which stabilizes its localization in centromeric regions during the S phase of the cell cycle. We then identified two residues in CENPA responsible for m6A recognition. Mutations in these CENPA residues or removal of m6A on cenRNAs leads to the loss of centromere-bound CENPA during the S phase, thereby resulting in abnormal chromosome separation during mitosis and increased genomic instability. Consequently, this impairment in centromere integrity hindered cancer cell proliferation and tumor growth. Our findings unveiled a novel m6A reading mechanism by CENPA that epigenetically governs centromere integrity in cancer cells, providing potentially new targets for cancer therapy.

2024-09-24 | GSE230879 | GEO

CENPA as a reader of m6A-modified centromeric RNA to ensure centromere integrity in cancer cells [MeRIP-seq]

2024-09-24 | GSE230877 | GEO

CENPA as a reader of m6A-modified centromeric RNA to ensure centromere integrity in cancer cells [RIP-Seq]

2024-09-24 | GSE247873 | GEO

CENPA as a reader of m6A-modified centromeric RNA to ensure centromere integrity in cancer cells [ChIRP-seq]

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Centromeric chromatin in mitosis reorganizes into a functional structure stabilized by cohesin [CENPA-ChIP-seq]

Project description:Three-dimensional organization of mitotic chromosomes is established by cohesin and condensin complexes. In the centromere, cohesin maintains sister chromatid pairing until anaphase onset, while condensin provides elastic resistance to spindle forces. However, how condensin and cohesin structure vertebrate centromeres remains unclear. By super-resolution imaging, Capture-C analysis and polymer modeling we show that vertebrate centromeres are partitioned into two condensin-dependent subdomains during mitosis. This bipartite sub-structure is found in human, mouse and chicken centromeres, and is therefore a fundamental feature of vertebrate centromere. Super-resolution imaging and electron tomography reveal that bipartite centromeres assemble bipartite kinetochores with each subdomain capable of binding a distinct microtubule bundle. Cohesin helps to link the centromere subdomains, limiting their separation in response to spindle forces and preventing merotelic attachments. The two-domain structure described here may have implications for avoiding chromosomal instability as uncoupling of centromere subdomains is a common feature of lagging chromosomes in cancer cells.

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Chromatin immunoprecipitation of centromeric protein CenpA from a human cell line containing a neocentromere in band 13q33.1

Project description:Chromatin Immunoprecipitation of Centromeric Protein CenpA from BBB a human cell line containing a neocentromere in band 13q33.1

2022-11-23 | E-TABM-294 | biostudies-arrayexpress

Chromatin immunoprecipitation of centromeric proteins CenpA and CenpC from human cell lines containing a neocentromere in band 13q21

Project description:Chromatin Immunoprecipitation of Centromeric Proteins, CenpA or CenpC, from human cell lines containing a neocentromere in band 13q21

2006-11-06 | E-TABM-168 | biostudies-arrayexpress

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