scholarly journals Human centromere protein A (CENP-A) can replace histone H3 in nucleosome reconstitution in vitro

2000 ◽  
Vol 97 (13) ◽  
pp. 7266-7271 ◽  
Author(s):  
K. Yoda ◽  
S. Ando ◽  
S. Morishita ◽  
K. Houmura ◽  
K. Hashimoto ◽  
...  
Keyword(s):  
Protein A ◽  
Histone H3 ◽  
Human Centromere ◽  
Centromere Protein ◽  
Centromere Protein A

scholarly journals CENP-A is phosphorylated by Aurora B kinase and plays an unexpected role in completion of cytokinesis

2001 ◽  
Vol 155 (7) ◽  
pp. 1147-1158 ◽  
Author(s):  
Samantha G. Zeitlin ◽  
Richard D. Shelby ◽  
Kevin F. Sullivan
Keyword(s):  
Protein A ◽  
Phosphorylation Site ◽  
Histone H3 ◽  
Dominant Negative ◽  
Aurora B ◽  
Human Centromere ◽  
Centromere Protein ◽  
Centromere Protein A ◽  
Chromosomal Passenger

Aurora B is a mitotic protein kinase that phosphorylates histone H3, behaves as a chromosomal passenger protein, and functions in cytokinesis. We investigated a role for Aurora B with respect to human centromere protein A (CENP-A), a centromeric histone H3 homologue. Aurora B concentrates at centromeres in early G2, associates with histone H3 and centromeres at the times when histone H3 and CENP-A are phosphorylated, and phosphorylates histone H3 and CENP-A in vitro at a similar target serine residue. Dominant negative phosphorylation site mutants of CENP-A result in a delay at the terminal stage of cytokinesis (cell separation). The only molecular defects detected in analysis of 22 chromosomal, spindle, and regulatory proteins were disruptions in localization of inner centromere protein (INCENP), Aurora B, and a putative partner phosphatase, PP1γ1. Our data support a model where CENP-A phosphorylation is involved in regulating Aurora B, INCENP, and PP1γ1 targeting within the cell. These experiments identify an unexpected role for the kinetochore in regulation of cytokinesis.

scholarly journals Constitutive centromere-associated network contacts confer differential stability on CENP-A nucleosomes in vitro and in the cell

2018 ◽  
Vol 29 (6) ◽  
pp. 751-762 ◽  
Author(s):  
Shengya Cao ◽  
Keda Zhou ◽  
Zhening Zhang ◽  
Karolin Luger ◽  
Aaron F. Straight
Keyword(s):  
Protein A ◽  
Histone H3 ◽  
Intrinsic Property ◽  
Cell Cycles ◽  
Centromere Protein A ◽  
Histone H3 Variant ◽  
Differential Stability ◽  
The Stability

Eukaryotic centromeres are defined by the presence of nucleosomes containing the histone H3 variant, centromere protein A (CENP-A). Once incorporated at centromeres, CENP-A nucleosomes are remarkably stable, exhibiting no detectable loss or exchange over many cell cycles. It is currently unclear whether this stability is an intrinsic property of CENP-A containing chromatin or whether it arises from proteins that specifically associate with CENP-A chromatin. Two proteins, CENP-C and CENP-N, are known to bind CENP-A human nucleosomes directly. Here we test the hypothesis that CENP-C or CENP-N stabilize CENP-A nucleosomes in vitro and in living cells. We show that 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.

scholarly journals Uracil DNA N-Glycosylase Promotes Assembly of Human Centromere Protein A

PLoS ONE ◽  
2011 ◽  
Vol 6 (3) ◽  
pp. e17151 ◽  
Author(s):  
Samantha G. Zeitlin ◽  
Brian R. Chapados ◽  
Norman M. Baker ◽  
Caroline Tai ◽  
Geir Slupphaug ◽  
...  
Keyword(s):  
Protein A ◽  
Human Centromere ◽  
Centromere Protein ◽  
Centromere Protein A

scholarly journals Active establishment of centromeric CENP-A chromatin by RSF complex

2009 ◽  
Vol 185 (3) ◽  
pp. 397-407 ◽  
Author(s):  
Marinela Perpelescu ◽  
Naohito Nozaki ◽  
Chikashi Obuse ◽  
Hua Yang ◽  
Kinya Yoda
Keyword(s):  
Protein A ◽  
Centromeric Chromatin ◽  
Daughter Cells ◽  
Centromere Protein ◽  
Centromere Protein A ◽  
Protein Components ◽  
And Function ◽  
Relationship Of ◽  
The Relationship

Centromeres are chromosomal structures required for equal DNA segregation to daughter cells, comprising specialized nucleosomes containing centromere protein A (CENP-A) histone, which provide the basis for centromeric chromatin assembly. Discovery of centromere protein components is progressing, but knowledge related to their establishment and maintenance remains limited. Previously, using anti-CENP-A native chromatin immunoprecipitation, we isolated the interphase–centromere complex (ICEN). Among ICEN components, subunits of the remodeling and spacing factor (RSF) complex, Rsf-1 and SNF2h proteins, were found. This paper describes the relationship of the RSF complex to centromere structure and function, demonstrating its requirement for maintenance of CENP-A at the centromeric core chromatin in HeLa cells. The RSF complex interacted with CENP-A chromatin in mid-G1. Rsf-1 depletion induced loss of centromeric CENP-A, and purified RSF complex reconstituted and spaced CENP-A nucleosomes in vitro. From these data, we propose the RSF complex as a new factor actively supporting the assembly of CENP-A chromatin.

Anti-centromere protein A antibodies in systemic sclerosis: Significance and origin

2016 ◽  
Vol 15 (1) ◽  
pp. 102-109 ◽  
Author(s):  
Federico Perosa ◽  
Marcella Prete ◽  
Giuseppe Di Lernia ◽  
Carmela Ostuni ◽  
Elvira Favoino ◽  
...  
Keyword(s):  
Systemic Sclerosis ◽  
Protein A ◽  
Centromere Protein ◽  
Centromere Protein A

scholarly journals Functional Complementation of Human Centromere Protein A (CENP-A) by Cse4p from Saccharomyces cerevisiae

2004 ◽  
Vol 24 (15) ◽  
pp. 6620-6630 ◽  
Author(s):  
Gerhard Wieland ◽  
Sandra Orthaus ◽  
Sabine Ohndorf ◽  
Stephan Diekmann ◽  
Peter Hemmerich
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Cycle ◽  
Cell Cycle Arrest ◽  
Budding Yeast ◽  
Protein A ◽  
Human Cells ◽  
Cycle Arrest ◽  
Centromere Protein ◽  
Centromere Protein A

ABSTRACT We have employed a novel in vivo approach to study the structure and function of the eukaryotic kinetochore multiprotein complex. RNA interference (RNAi) was used to block the synthesis of centromere protein A (CENP-A) and Clip-170 in human cells. By coexpression, homologous kinetochore proteins from Saccharomyces cerevisiae were then tested for the ability to complement the RNAi-induced phenotypes. Cse4p, the budding yeast CENP-A homolog, was specifically incorporated into kinetochore nucleosomes and was able to complement RNAi-induced cell cycle arrest in CENP-A-depleted human cells. Thus, Cse4p can structurally and functionally substitute for CENP-A, strongly suggesting that the basic features of centromeric chromatin are conserved between yeast and mammals. Bik1p, the budding yeast homolog of human CLIP-170, also specifically localized to kinetochores during mitosis, but Bik1p did not rescue CLIP-170 depletion-induced cell cycle arrest. Generally, the newly developed in vivo complementation assay provides a powerful new tool for studying the function and evolutionary conservation of multiprotein complexes from yeast to humans.

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