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centromere assembly factors CAL1 (show CALCA Proteins) and CENP-C are required for meiotic chromosome segregation, CENP-A assembly and maintenance on sperm, as well as fertility
identify two co-evolving regions, CENP-A L1 and the CAL1 (show CALCA Proteins) N terminus, as critical for lineage-specific CENP-A incorporation
A novel role has been described for the histone acetyltransferase Hat1 (show HAT1 Proteins) in the CENP-A/CID assembly pathway in Drosophila melanogaster.
CENP-A assembly by its loading factor, CAL1, requires RNAPII-mediated transcription of the underlying DNA
The amount of Cid that is loaded during each cell cycle appears to be determined primarily by the preexisting centromeric Cid, with little flexibility for compensation of accidental losses.
CID nucleosomes are octameric in vivo and that CID dimerization is essential for correct centromere assembly.
The F box protein (show FBXO30 Proteins) partner of paired (Ppa (show FBXL14 Proteins)) mediates CenH3(CID) stability in Drosophila. Ppa (show FBXL14 Proteins) depletion results in increased CenH3(CID) levels. Ppa (show FBXL14 Proteins) physically interacts with CenH3(CID) through the CATD (show CTSD Proteins)(CID) that mediates Ppa (show FBXL14 Proteins)-dependent CenH3(CID) stability.
Drosophila CENP-C is essential for centromere identity.
Cid allows for contacts betwen DNA and histones and specific targeting
Results suggest that CID mislocalization promotes formation of ectopic centromeres and multicentric chromosomes, which causes chromosome missegregation, aneuploidy, and growth defects.
Identify the licensing factor M18BP1 (show MIS18BP1 Proteins) and the CENP-A chaperone HJURP (show HJURP Proteins) as the two key targets of Cdk (show CDK4 Proteins)-based inhibition sufficient for maintenance of strict cell-cycle control of CENP-A assembly.
CENP-A specifically binds alpha satellite non-coding RNAs. Loss of CENP-A does not affect transcript abundance or stability.
Evolutionarily conserved flexible ends of the CENP-A nucleosomes are essential to ensure the fidelity of the mitotic pathway.
These data implicate the insulin (show INS Proteins)-FoxM1 (show FOXM1 Proteins)/PLK1/CENP-A pathway-regulated mitotic cell-cycle progression as an essential component in the beta cell adaptation to delay and/or prevent progression to diabetes.
Findings indicate that expression of the scleroderma autoantigens IFI-16 (show IFI16 Proteins) and CENPs (show APITD1 Proteins), which are associated with severe vascular disease, is increased in vascular progenitors and mature endothelial cells. High level, lineage-enriched expression of autoantigens may explain the striking association between clinical phenotypes and the immune targeting of specific autoantigens.
KAT7 (show MYST2 Proteins)-containing acetyltransferases associating with the Mis18 complex provides competence for histone turnover/exchange activity on alphoid DNA and prevents Suv39h1 (show SUV39H1 Proteins)-mediated heterochromatin invasion into centromeres.
CENP-A mutants that cannot be phosphorylated at Ser68 or ubiquitinated at Lys124 assemble efficiently at centromeres during G1, mediate early events in centromere establishment at an ectopic chromosomal locus, and maintain centromere function indefinitely.
elevated CENP-A expression is coupled to malignant progression of numerous types of cancer. It may be useful as a biomarker of poor patient prognosis and as a predictive biomarker for taxane-based chemotherapy.
CENP-C and CENP-I (show CENPI Proteins) are key factors connecting kinetochore to CENP-A assembly.
The authors found that the nucleosome shape change directed by CENP-A is dominated by lateral passing of two DNA gyres (gyre sliding).
evolutionarily conserved flexible ends of the CENP-A nucleosomes are essential to ensure the fidelity of the mitotic pathway.
CPCs maintain relatively high levels of CENP-A early in life, which is necessary for sustaining proliferation, inhibiting senescence, and promoting survival following differentiation of CPCs.
Results report that the level of CENP-A, a protein required for cell division, declines precipitously with age in an islet-specific manner.
Cenpa, Cenpb (show CENPB Proteins), and Bub3 (show BUB3 Proteins), but not Cenpc, interacted with PARP-1 (show PARP1 Proteins)
The centromere-targeting domain of CENP-A is both necessary and sufficient for recruitment to double-strand breaks. CENP-A accumulation at DNA breaks is enhanced by active non-homologous end-joining but does not require DNA-PKcs (show PRKDC Proteins) or Ligase IV.
CENP-C and M18BP1 (show MIS18BP1 Proteins) recruit HJURP (show HJURP Proteins) to centromeres for new CENP-A assembly.
CENP-A assembly into chromatin requires unidentified deoxycytidine deaminase (show APOBEC3G Proteins) and UNG2 (show CCNO Proteins), a uracil DNA glycosylase (show UNG Proteins).
CENP-A deposition at the centromeres is dependent on HJURP (show HJURP Proteins).
Centromeres are the differentiated chromosomal domains that specify the mitotic behavior of chromosomes. CENPA encodes a centromere protein which contains a histone H3 related histone fold domain that is required for targeting to the centromere. CENPA is proposed to be a component of a modified nucleosome or nucleosome-like structure in which it replaces 1 or both copies of conventional histone H3 in the (H3-H4)2 tetrameric core of the nucleosome particle. Alternative splicing results in multiple transcript variants encoding distinct isoforms.
, centromere identifier protein
, centromere protein A
, centromere protein-A
, centromere protein, Xenopus
, histone H3-like centromeric protein A
, centromeric histone-3 like protein
, centromere autoantigen A
, centromere protein A, 17kDa
, centromere-specific histone
, centrosomin A