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H3.3 chaperones HIRA and DAXX promote ectopic CENP-A deposition.
phosphorylation of CENP-A on serine 7 dispensable to correct centromere dynamics and function
CENP-N stabilizes CENP-A nucleosomes alone and additively with CENP-C in vitro. However, removal of CENP-C and CENP-N from cells, or mutating CENP-A so that it no longer interacts with CENP-C or CENP-N, had no effect on centromeric CENP-A stability in vivo. Thus, the stability of CENP-A nucleosomes in chromatin does not arise solely from its interactions with CENP-C or CENP-N.
Aurora A-dependent phosphorylation of CENP-A at the inner centromere protects chromosomes against tension-induced cohesion fatigue until the last kinetochore is attached to spindle microtubules.
CENP-A undergoes alpha-amino trimethylation by the enzyme NRMT in vivo.
H4K5ac and H4K12ac, mediated by RbAp46/48, facilitates efficient CENP-A deposition into centromeres.
Collectively, these studies clarify how CENP-N and CENP-C decode and stabilize the non-canonical CENP-A nucleosome to enforce epigenetic centromere specification and kinetochore assembly.
the SGT1-HSP90 complex contributes to the E3 ligase activity of the CUL4A complex that is necessary for CENP-A ubiquitylation and CENP-A deposition at the centromere.
during the CENP-A/H4 deposition process, the chaperone HJURP protects various substructures of the dimer, serving both as a folding and binding chaperone
This study provides insights into how overexpression of CENP-A may contribute to CIN in cancers and underscore the importance of understanding the pathways that prevent CENP-A mislocalization for genome stability.
Findings indicate the role of the amino-terminus of centromere protein A (CENP-A) in localization.
Levels of centromere aberrations increase upon depletion of CENP-A, CENP-C, and CENP-T/W, during replicative senescence, and in cancer cells.
findings demonstrate the involvement of consensus Cdk1 phosphorylation sites on Mis18 complex assembly and thus provide a rationale for cell cycle-regulated timing of Mis18 assembly and CENP-A deposition
Upon cross-linking, the entire CENPA/CENPB/CENPC/CENPT complex is nuclease-protected over an alpha-satellite dimer that comprises the fundamental unit of centromeric chromatin. We conclude that CENPA/CENPC and CENPT pathways for kinetochore assembly are physically integrated over young alpha-satellite dimers.
we review our current understanding of CENP-A evolution in relation to centromere drive and discuss classical and recent advances, including new evidence implicating CENP-A chaperones in this conflict.
there is a reciprocal interdependency of CENP-A chromatin and the underlying repetitive centromere DNA sequences bound by CENP-B in the maintenance of human chromosome segregation.
Identify the licensing factor M18BP1 and the CENP-A chaperone HJURP as the two key targets of Cdk-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-FoxM1/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.
CENP-A nucleosome retention at centromeres requires a core centromeric nucleosome complex where CENP-C clamps down a stable nucleosome conformation and CENP-N fastens CENP-A to the DNA.
Centromeres with more satellite repeats house more nucleosomes that confer centromere identity, containing the histone H3 variant CENP-A, and bias their segregation to the egg relative to centromeres with fewer repeats.
The findings provide evidence that CENP-A is critical for the faithful chromosome segregation during mammalian oocyte meiosis.
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, and Bub3, but not Cenpc, interacted with PARP-1
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 or Ligase IV.
CENP-C and M18BP1 recruit HJURP to centromeres for new CENP-A assembly.
CENP-A assembly into chromatin requires unidentified deoxycytidine deaminase and UNG2, a uracil DNA glycosylase.
CENP-A deposition at the centromeres is dependent on HJURP.
XCENP-A associates with frog centromeric repeat 1.
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 autoantigen A
, centromere protein A, 17kDa
, centromere-specific histone
, histone H3-like centromeric protein A
, centrosomin A
, centromere protein, Xenopus
, centromeric histone-3 like protein
, centromere protein A