Calreticulin as a new histone binding protein in mitotic chromosomes

2006 ◽  
Vol 115 (1) ◽  
pp. 10-15 ◽  
Author(s):  
S. Kobayashi ◽  
S. Uchiyama ◽  
T. Sone ◽  
M. Noda ◽  
L. Lin ◽  
...  
Keyword(s):  
Binding Protein ◽  
Mitotic Chromosomes ◽  
Histone Binding

scholarly journals Molecular Mechanism for Age-Related Memory Loss: The Histone-Binding Protein RbAp48

2013 ◽  
Vol 5 (200) ◽  
pp. 200ra115-200ra115 ◽  
Author(s):  
E. Pavlopoulos ◽  
S. Jones ◽  
S. Kosmidis ◽  
M. Close ◽  
C. Kim ◽  
...  
Keyword(s):  
Molecular Mechanism ◽  
Binding Protein ◽  
Memory Loss ◽  
Histone Binding ◽  
Age Related

scholarly journals A Variant of the Histone-Binding Protein sNASP Contributes to Mouse Lupus

2019 ◽  
Vol 10 ◽  
Author(s):  
Jiyu Ju ◽  
Jia Xu ◽  
Yaoqiang Zhu ◽  
Xiaoyan Fu ◽  
Laurence Morel ◽  
...  
Keyword(s):  
Binding Protein ◽  
Histone Binding

scholarly journals Dynamic Localization of the Human Papillomavirus Type 11 Origin Binding Protein E2 through Mitosis While in Association with the Spindle Apparatus

2006 ◽  
Vol 80 (10) ◽  
pp. 4792-4800 ◽  
Author(s):  
Luan D. Dao ◽  
Aaron Duffy ◽  
Brian A. Van Tine ◽  
Shwu-Yuan Wu ◽  
Cheng-Ming Chiang ◽  
...  
Keyword(s):  
Human Papillomavirus ◽  
Binding Protein ◽  
Cellular Protein ◽  
Bovine Papillomavirus ◽  
Mitotic Spindles ◽  
Mitotic Chromosomes ◽  
Mitotic Apparatus ◽  
Viral Origin ◽  
E2 Protein ◽  
Origin Binding Protein

ABSTRACT Papillomaviral DNA replicates as extrachromosomal plasmids in squamous epithelium. Viral DNA must segregate equitably into daughter cells to persist in dividing basal/parabasal cells. We have previously reported that the viral origin binding protein E2 of human papillomavirus types 11 (HPV-11), 16, and 18 colocalized with the mitotic spindles. In this study, we show the localization of the HPV-11 E2 protein to be dynamic. It colocalized with the mitotic spindles during prophase and metaphase. At anaphase, it began to migrate to the central spindle microtubules, where it remained through telophase and cytokinesis. It was additionally observed in the midbody at cytokinesis. A peptide spanning residues 285 to 308 in the carboxyl-terminal domain of HPV-11 E2 (E2C) is necessary and sufficient to confer localization on the mitotic spindles. This region is conserved in HPV-11, -16, and -18 and bovine papillomavirus type 4 (BPV-4) E2 and is also required for the respective E2C to colocalize with the mitotic spindles. The E2 protein of bovine papillomavirus type 1 is tethered to the mitotic chromosomes via the cellular protein Brd4. However, the HPV-11 E2 protein did not associate with Brd4 during mitosis. Lastly, a chimeric BPV-1 E2C containing the spindle localization domain from HPV-11 E2C gained the ability to localize to the mitotic spindles, whereas the reciprocal chimera lost the ability. We conclude that this region of HPV E2C is critical for localization with the mitotic apparatus, enabling the HPV DNA to sustain persistent infections.

Characterization of the Testicular Histone-Binding Protein, NASP

The Testis ◽  
2000 ◽  
pp. 143-150 ◽  
Author(s):  
Michael G. O’Rand ◽  
Iglika N. Batova ◽  
Richard T. Richardson
Keyword(s):  
Binding Protein ◽  
Histone Binding

scholarly journals Overexpression of the Linker Histone-binding Protein tNASP Affects Progression through the Cell Cycle

2002 ◽  
Vol 278 (10) ◽  
pp. 8846-8852 ◽  
Author(s):  
Oleg M. Alekseev ◽  
David C. Bencic ◽  
Richard T. Richardson ◽  
Esther E. Widgren ◽  
Michael G. O'Rand
Keyword(s):  
Cell Cycle ◽  
Binding Protein ◽  
Linker Histone ◽  
Histone Binding

scholarly journals Histone Binding Protein RbAp48 Interacts with a Complex of CREB Binding Protein and Phosphorylated CREB

2000 ◽  
Vol 20 (14) ◽  
pp. 4970-4978 ◽  
Author(s):  
Qinghong Zhang ◽  
Ngan Vo ◽  
Richard H. Goodman
Keyword(s):  
Transcriptional Activation ◽  
Binding Protein ◽  
In Vitro Transcription ◽  
Dependent Manner ◽  
Creb Binding Protein ◽  
Histone Binding ◽  
Nuclear Extracts ◽  
Core Histones ◽  
Phosphorylated Creb

ABSTRACT A CREB-CREB binding protein (CBP) complex was used as bait to screen a mouse embryo cDNA library in yeast. One of the strongest interactions identified the histone binding protein RbAp48. RbAp48 also interacted weakly with CBP alone but did not interact with phosphorylated or nonphosphorylated CREB. CBP (or its homologue p300) from HeLa cell nuclear extracts coimmunoprecipitated with RbAp48 and its homologue RbAp46 and bound to a glutathioneS-transferase–RbAp48 fusion protein. This interaction was stimulated by the addition of phosphorylated CREB and allowed the association of core histones and mononucleosomes in an acetylation-dependent manner. RbAp48 lowered theKm of CBP histone acetylase activity and facilitated p300-mediated in vitro transcription of a chromatinized template in the presence of acetylcoenzyme A. These data indicate that the association of phosphorylated CREB with CBP promotes the binding of RbAp48 and its homologue RbAp46, allowing the formation of a complex that facilitates histone acetylation during transcriptional activation.

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