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Human Polyclonal CENPA Primary Antibody pour DB, ICC - ABIN2668362
Logsdon, Barrey, Bassett, DeNizio, Guo, Panchenko, Dawicki-McKenna, Heun, Black: Both tails and the centromere targeting domain of CENP-A are required for centromere establishment. dans The Journal of cell biology 2015
High-speed atomic force microscopy was used for direct visualization of the spontaneous dynamics of centromere protein A (CENP-A)nucleosomes at the sub-second time scale.
Using genome-wide mapping and reference models for 23 human centromeres, CENP-A binding sites are identified within the megabase-long, repetitive alpha-satellite DNAs at each centromere. CENP-A is shown in early G1 to be assembled into nucleosomes within each centromere and onto 11,390 transcriptionally active sites on the chromosome arms
Results showed that CENPA, CDK1 and CDC20 were highly expressed in lung adenocarcinoma (LAC) tissue with co-expression patterns. Also, the integrated microarray analysis demonstrated that CENPA, CDK1 and CDC20 might serve as novel cluster of prognostic biomarkers for LAC.
Study determined the cryo-electron microscopy structure of the human centromeric nucleosome containing CENP-A and a native alpha-satellite DNA sequence at 2.6 A resolution.
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.
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.
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.
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