Tammar wallaby CENP-A ChIP-seq
Ontology highlight
ABSTRACT:
ORGANISM(S): Macropus eugenii
SUBMITTER: James Lindsay
PROVIDER: E-GEOD-30371 | biostudies-arrayexpress |
REPOSITORIES: biostudies-arrayexpress
Similar Datasets
Project description:Chromatin immunoprecipitation from tammar wallaby pouch young cells for DNA bound to CENP-A
2011-07-28 | GSE30371 | GEO
Project description:We find that CENP-T acts as a bridge between two well-positioned CENP-A nucleosomes that are present on young alpha-satellite dimers that dominate functional human centromeres. CENP-T is centered over the CENP-B box, where it interacts with the CENP-B/CENP-C complex. Upon cross-linking, the entire CENP-A/CENP-C/CENP-T-containing complex is recovered as a nuclease-protected particle over an alpha-satellite dimer that comprises the fundamental unit of kinetochore chromatin. Our work reveals that CENP-A/CENP-C and CENP-T branches of kinetochore assembly are physically integrated.
2016-05-24 | GSE69839 | GEO
Project description:B. cenocepacia J2315 was grown on LB medium to mid-stationary phase at OD 0.3 under full aeration and then transferred into a 50 ml centrifuge tube and placed upright into a CampyGen Compact (Oxoid, Basingstoke, UK) plastic pouch containing the gas generating paper sachet. The pouch was sealed immediately and then the cap of the centrifuge tube loosened to allow exchange of atmosphere between centrifuge tube and pouch. <br>The culture was further incubated at 37 degrees centigrade and 150 rpm for 2-3 hours until it reached OD 0.5. The centrifuge tube was sealed before opening the pouch and then snap-cooled before harvest to minimise exposure to atmospheric oxygen and to ensure expression profiles reflect the lower oxygen concentration.<br>The expression profile was compared to cells grown to OD 0.5 at atmospheric oxygen concentrations.<br>
2012-01-01 | E-MEXP-2787 | biostudies-arrayexpress
Project description:Mast cells (MCs) were implicated in tissue remodelling in hamster models of heart inflammatory diseases. Here we asked whether MCs promote inflammatory neovascularization in hamster cheek pouch (HCP) parasitized by Trypanosoma cruzi, the protozoan that causes Chagas disease. Intravital microscopy (IVM) performed 3 days after inoculation of Dm28c trypomastigote (GFP-TCTs) showed a subtle infiltration of rhodamine-labeled leukocytes. Interestingly, the baseline levels of FITC-dextran leakage (3 dpi) were consistently increased, raising the possibility that intracellular amastigotes may coopt the low-grade inflammation to facilitate the delivery of plasma-borne nutrients during the period in which host cells must metabolically sustain parasite division. Although proangiogenic indexes were only mildly stimulated at 3 dpi, we found a positive correlation with transcription of proinflammatory cytokines (pro-IL- and IFN-). Having established 3 dpi as a timepoint in which vascular remodeling was already measurable, we next compared the proteomic profiles of parasitized HCP with those of internal controls (PBS injected 3 days earlier in the contralateral pouch) we found 87 proteins upregulated, and 17 were downregulated in the parasitized HCP. Minor changes in protein expression were observed in response to PBS injection (2 upregulated and 12 downregulated proteins. Congruent with the increased density of MCs observed in parasitized HCP (histological analysis), the MC protease 1 (chymase) stood out as the most abundant sequence. Interestingly, toluidine blue staining appointed clusters of MCs degranulating at 3 dpi. Noteworthy, two plasma proteins (complement C3 and serum albumin) were also identified as major proteins, further suggesting that leaky capillaries irrigated the HCP at early stages (3 dpi) of infection . Detection of cytokines or classical proangiogenic factors was beyond the sensitivity of our methods.
2022-04-04 | PXD026905 | Pride
Project description:Restricting the localization of the centromeric histone H3 variant CENP-A to centromeres is essential to prevent chromosomal instability (CIN). Mislocalization of overexpressed CENP-A contributes to CIN in yeast, fly, and human cells. CENP-A is overexpressed in many cancers. Therefore, defining mechanisms that prevent CENP-A mislocalization will help us understand how CENP-A overexpression contributes to CIN in cancer. A genome-wide screen to characterize essential genes required for growth when CENP-A is overexpressed identified the replication initiation Dbf4-Dependent Kinase (DDK) complex. We show that DDK regulates ubiquitin-mediated proteolysis of Cse4 and prevents mislocalization of Cse4 independently of its role in DNA replication.
2020-04-04 | GSE148068 | GEO
Project description:ChIP-seq of CENP-A in S. pombe
2013-01-04 | E-MTAB-1435 | biostudies-arrayexpress
Project description:CENP-A is a centromere-specific histone 3 variant essential for centromere specification. CENP-A partially replaces canonical histone H3 at the centromeres. How the particular CENP-A/H3 ratio at centromeres is precisely maintained is unknown. It also remains unclear how CENP-A is excluded from non-centromeric chromatin. Here we identify Ccp1, an uncharacterized NAP family protein in fission yeast that antagonizes CENP-A loading at both centromeric and non-centromeric regions. Like the CENP-A loading factor HJURP, Ccp1 interacts with CENP-A, and is recruited to centromeres at the end of mitosis in a Mis16-dependent manner. These data indicate that factors with opposing CENP-A loading activities are recruited to centromeres. Furthermore, Ccp1 also cooperates with H2A.Z to evict CENP-A assembled in euchromatin. Structural analyses indicate that Ccp1 forms a homodimer that is required for its anti-CENP-A loading activity. Our study establishes mechanisms for maintenance of CENP-A homeostasis at centromeres and the prevention of ectopic assembly of centromeres. Examination of cnp1 distribution in one wild type (wt) and two ccp1 mutants.
2016-08-04 | E-GEOD-85166 | biostudies-arrayexpress
Project description:Centromeric localization of the evolutionarily conserved histone H3 variant, CENP-A. is essential for chromosomal stability. CENP-A overexpression (OE) causesd its mislocalization to non-centromeric regions resulting in chromosomal instability (CIN) in yeast, flies and human cells. CENP-A OE and mislocalization have been observed in cancers and correlates with poor prognosis. However, the molecular consequences of CENP-A OE on CIN and aneuploidy have not been defined. Here, we overexpressed YFP-CENP-A in a pseudodiploid DLD1 cell line and showed that CENP-A OE leads to its mislocalization and CIN due to defects in kinetochore integrity and kinetochore-microtubule attachments. CENP-A OE also leads to its mislocalization and CIN in a xenograft mouse model. Under these conditions, it contributes to aneuploidy with karyotypic heterogeneity in human cells and xenograft mouse model. In summary, our studies provide a molecular link between CENP-A OE and aneuploidy, and suggest that karyotypic heterogeneity may contribute to the aggressive phenotype of CENP-A overexpressing cancers.
2020-07-16 | GSE154460 | GEO
Project description:CENP-A is a centromere-specific histone 3 variant essential for centromere specification. CENP-A partially replaces canonical histone H3 at the centromeres. How the particular CENP-A/H3 ratio at centromeres is precisely maintained is unknown. It also remains unclear how CENP-A is excluded from non-centromeric chromatin. Here we identify Ccp1, an uncharacterized NAP family protein in fission yeast that antagonizes CENP-A loading at both centromeric and non-centromeric regions. Like the CENP-A loading factor HJURP, Ccp1 interacts with CENP-A, and is recruited to centromeres at the end of mitosis in a Mis16-dependent manner. These data indicate that factors with opposing CENP-A loading activities are recruited to centromeres. Furthermore, Ccp1 also cooperates with H2A.Z to evict CENP-A assembled in euchromatin. Structural analyses indicate that Ccp1 forms a homodimer that is required for its anti-CENP-A loading activity. Our study establishes mechanisms for maintenance of CENP-A homeostasis at centromeres and the prevention of ectopic assembly of centromeres.
2016-08-04 | GSE85166 | GEO