Fission yeasts CENPA and H3K9me Chip-seq
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA447408 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR6910790.fastq.gz | Fastqsanger.gz | |||
| SRR6910800_1.fastq.gz | Fastqsanger.gz | |||
| SRR6910800_2.fastq.gz | Fastqsanger.gz | |||
| SRR6910791_1.fastq.gz | Fastqsanger.gz | |||
| SRR6910791_2.fastq.gz | Fastqsanger.gz |
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Project description:Centromeres are the regions of eukaryotic chromosomes where kinetochores are assembled and direct the correct segregation of chromosomes. Active centromeres are defined by presence of nucleosomes containing CENP-A, a histone H3 variant, which alone is sufficient to direct kinetochore assembly. Once assembled at a location CENP-A chromatin and the kinetochore is maintained at that location though a positive feedback loop where kinetochore proteins recruited by CENP-A promote deposition of new CENP-A following replication. Although CENP-A chromatin itself is a heritable entity, it is normally associated with specific sequences such as human alpha satellite arrays. Such analyses suggest that properties of centromeric DNA itself may favour assembly of CENP-A rather than H3 nucleosomes. To investigate the innate properties of centromeric DNA we have examined histone dynamics on this DNA assembled in CENP-A chromatin at endogenous centromeres and when assembled only in H3 chromatin at an ectopic location. We demonstrate that H3 occupancy on centromeric DNA is innately low while H3 turnover is high. Moreover, even at an ectopic location centromeric DNA programs H3 deposition in S phase and its eviction during G2 when CENP-A is otherwise deposited. G2 accumulation of RNAPII on centromeric DNA during G2 is consistent with transcription-coupled destabilisation of H3 nucleosomes to favour CENP-A deposition.
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Project description:Overexpression of centromeric proteins has been identified in a number of human malignancies, though their functional and mechanistic contributions to disease progression have not been characterized. CENPA, the centromeric histone H3 variant, is the epigenetic mark that determines centromere identity. Here, we demonstrate that CENPA is highly overexpressed in prostate cancer in both tissue and cell lines, and the level of CENPA expression correlates with the stage of disease. Gain-of- and loss-of-function experimentation confirms that CENPA promotes prostate cancer cell line growth. Integrated sequencing studies further reveal a previously unidentified function of CENPA as a transcriptional regulator that modulates expression of critical proliferation, cell-cycle, and centromere/kinetochore genes. Our findings, therefore, suggest a previously undescribed biological function for CENPA, a protein normally thought to be solely and importantly involved in centromere identity.
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Project description:Overexpression of centromeric proteins has been identified in a number of human malignancies, though their functional and mechanistic contributions to disease progression have not been characterized. CENPA, the centromeric histone H3 variant, is the epigenetic mark that determines centromere identity. Here, we demonstrate that CENPA is highly overexpressed in prostate cancer in both tissue and cell lines, and the level of CENPA expression correlates with the stage of disease. Gain-of- and loss-of-function experimentation confirms that CENPA promotes prostate cancer cell line growth. Integrated sequencing studies further reveal a previously unidentified function of CENPA as a transcriptional regulator that modulates expression of critical proliferation, cell-cycle, and centromere/kinetochore genes. Our findings, therefore, suggest a previously undescribed biological function for CENPA, a protein normally thought to be solely and importantly involved in centromere identity.
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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.
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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.
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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.
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