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 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 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

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.

scholarly journals Centromere protein A dynamics in human pluripotent stem cell self-renewal, differentiation and DNA damage

2010 ◽  
Vol 19 (20) ◽  
pp. 3970-3982 ◽  
Author(s):  
Gayane Ambartsumyan ◽  
Rajbir K. Gill ◽  
Silvia Diaz Perez ◽  
Deirdre Conway ◽  
John Vincent ◽  
...  
Keyword(s):  
Dna Damage ◽  
Stem Cell ◽  
Pluripotent Stem Cell ◽  
Protein A ◽  
Human Pluripotent Stem Cell ◽  
Self Renewal ◽  
Centromere Protein ◽  
Centromere Protein A

scholarly journals Anticentromere antibody induced by immunization with centromere protein a and Freund’s complete adjuvant may interfere with mouse oocyte meiosis

2021 ◽  
Vol 19 (1) ◽  
Author(s):  
Ying Ying ◽  
Shuang Liu ◽  
Yixuan Wu ◽  
Sichen Li ◽  
Qing Huang
Keyword(s):  
Protein A ◽  
Underlying Mechanism ◽  
Saline Group ◽  
Immunofluorescence Assay ◽  
Enzyme Linked Immunosorbent Assay ◽  
Control Groups ◽  
Anticentromere Antibody ◽  
Centromere Protein ◽  
Centromere Protein A ◽  
Oocyte Meiosis

Abstract Background Anticentromere antibody (ACA) is a member of the antinuclear antibody (ANA) family, and recent studies have found that ACA may be associated with oocyte maturation disorders; however, the possible mechanism behind this phenomenon remains unknown. We conducted this study to investigate whether ACA could penetrate into the living oocytes and interfere with oocyte meiosis in a mouse model. Methods We divided mice into three groups: human recombinant centromere protein-A (human CENP-A, HA) and complete Freund’s adjuvant (CFA) were used to immunize mice for the study group (HA + CFA), and mice injected with CFA (CFA group) or saline (Saline group), respectively, served as controls. After immunization, serum anti-CENP-A antibody was detected by indirect immunofluorescence assay (IIFT) and enzyme-linked immunosorbent assay (ELISA). Chromosome alignment and intracellular IgG localization in MI- and MII-stage oocytes were investigated by immunofluorescence analysis. Results Positive ACAs were successfully induced by immunization with CENP-A and CFA, and results showed that the serum level of anti-CENP-A antibody was significantly higher in the HA + CFA group compared with the control groups. There was marked increase of chromosome misalignments in MI and MII oocytes in the HA + CFA group compared to the control groups. However, no oocytes from any of the three groups showed intracellular antibody immunofluorescence. Conclusions The development and maturation of oocytes were impaired in peripheral ACA positive mice, which exhibited severe chromosomal misalignments in metaphase meiosis; however, no evidence of ACAs entering the oocytes was observed, thus the underlying mechanism needs further exploration.

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