• Journal of the Korean Chemical Society
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• v.29 no.3
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• pp.304-310
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• 1985

Effect of spermine on the susceptibility of calf thymus nucleohistone to DNase 1, in relation to the structural change of the nucleohistone, and cooperativity of the interaction of the nucleohistone with DNase 1 was investigated. Dansylated nucleohistone, in which the histone moiety had been derivatized by dansylation, was also used to investigate functional roles of the histone moiety on the cooperativity. The data here indicate the possibility that the nucleohistone, in contrast with the DNA, may not undergo monomolecular condensation, whereas intermolecular aggregation and enhancement of the positive cooperativity of the interaction of nucleohistone with DNase 1 may be brought about by spermine. The interaction of the DNS-nucleohistone with DNase 1 showed negative cooperativity. Based on the data here, it can be speculated that the cooperativity of the nucleohistone is influenced by the histone moiety of the nucleohistone.

• Bulletin of the Korean Chemical Society
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• v.24 no.5
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• pp.547-551
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• 2003

In the present work, the interaction of three water soluble porphyrins, tetra(p-trimethyle) ammonium phenyl porphyrin iodide (TAPP) as a cationic porphyrin, tetra sodium meso-tetrakis (p-sulphonato phenyle) porphyrin (TSPP) as an anionic porphyrin and manganese tetrakis (p-sulphonato phenyl) porphinato acetate (MnTSPP) as a metal porphyrin, with histone H₂B have been studied by isothermal titration microcalorimetry at 8 mM phosphate buffer, pH 6.8 and 27 °C. The values of binding constant, entropy, enthalpy and Gibbs free energy changes for binding of the first MnTSPP, and first and second TSPP and TAPP molecules were estimated from microcalorimetric data analysis. The results represent that the process is both entropy and enthalpy driven and histone induces self-aggregation of the porphyrins. The results indicate that both columbic and hydrophobic interactions act as self-aggregation driving forces for the formation of aggregates around histone.

• Animal cells and systems
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• v.16 no.4
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• pp.289-294
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• 2012

Histone methylation has diverse functions including transcriptional regulation via its lysine or arginine residue methylation. Studies indicate that deregulation of histone methylation is linked to human cancers including leukemia. Histone H3K27 methyltrnasferase response element II binding protein (RE-IIBP), as a transcriptional repressor to target gene IL-5, interacts with HDAC and is over-expressed in leukemia patient samples. In this study, we have identified that hematopoiesis-related genes GATA1 and HOXA9 are down-regulated by RE-IIBP in K562 and 293T cells. Transient reporter analysis revealed that GATA1 transcription was repressed by RE-IIBP. On the other hand, HOXA9 and PBX-related homeobox gene MEIS1 was up-regulated by RE-IIBP. These results suggest that RE-IIBP might have a role in hematopoiesis or leukemogenesis by regulating the transcription of target genes, possibly via its H3K27 methyltransferase activity.

• Bulletin of the Korean Chemical Society
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• v.33 no.6
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• pp.2063-2066
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• 2012

• Proceedings of the PSK Conference
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• 2003.10b
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• pp.184.1-184.1
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• 2003

HDAC and HAT (histone acetyltransferase) are involved in co-regulation in chromatin remodeling and the functional regulation of gene transcription. Abnormal recruitment of HDAC is related to carcinogenesis. Thus, the identification of potent histone deacetylase (HDAC) inhibitor has been considered as very intriguing approach for development for cancer chemotherapy. More recently, anti-inflammatory activity of SAHA cytokines was reported via reduction of proinflammatory cytokinres in vitro and in vivo. (omitted)

• Molecules and Cells
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• v.28 no.3
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• pp.149-154
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• 2009

Faithful and accurate replication of the DNA molecule is essential for eukaryote organisms. Nonetheless, in the last few years it has become evident that inheritance of the chromatin states associated with different regions of the genome is as important as the faithful inheritance of the DNA sequence itself. Such chromatin states are determined by a multitude of factors that act to modify not only the DNA molecule, but also the histone proteins associated with it. For instance, histones can be posttranslationally modified, and it is well established that these posttranslational marks are involved in several essential nuclear processes such as transcription and DNA repair. However, recent evidence indicates that posttranslational modifications of histones might be relevant during DNA replication. Hence, the aim of this review is to describe the most recent publications related to the role of histone posttranslational modifications during DNA replication.

• Journal of Microbiology and Biotechnology
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• v.3 no.3
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• pp.156-160
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• 1993

A chicken H2B histone gene was cloned and expressed in Rat 3 cell line. Its messenger RNA level was about 10 times higher during S phase than during $G_1$ phase. A chimeric chicken-yeast-chicken H2B histone gene was made to change some of wobble sequences of chicken H2B gene. When the chimeric H2B gene was transfected into the Rat 3 cell line, it showed a pattern of expression similar to that of the original chicken H2B gene. At least in this gene, it was concluded that the wobble sequences were not required for the cell-cycle regulated pattern of expression.

• Journal of Integrative Natural Science
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• v.6 no.1
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• pp.57-63
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• 2013

Histone deacetylase (HDACs) is an enzyme family that deacetylates histones and non-histones protein. Availability of crystal structure of HDAC8 has been a boosting factor to generate target based inhibitors. Hydroxamic class is the most studied one to generate potent inhibitors. HDAC class I and class II enzymes are emerging as a therapeutic target for cancer, diabetes, inflammation and other diseases. DNA methylation and histone modification are epigenetic mechanism, is important for the regulation of cellular functions. HDACs enzymes play essential role in gene transcription to regulate cell proliferation, migration and death. The aim of this article is to provide a comprehensive overview about structure and function of HDACs enzymes, histone deacetylase inhibitors (HDACi) and HDACs enzymes as a therapeutic target for cancer, inflammation and diabetes.

• Journal of Microbiology and Biotechnology
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• v.4 no.4
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• pp.274-277
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• 1994

We subcloned two chicken H3 histone genes and transfected them into Rat 3 cell line. One contains 300 bp 5' to its cap site and the other contains 130 bp 5' to its cap site when cloned into plasm ids. Both of them showed 5' phase specific expression of their mRNA about 8 fold higher (during 5' phase) than during Gl phase. This means that only 130 bp 5' to its cap site was enough to confer cell cycle regulated expression of the latter gene. The DNA sequences of their 5' flanking region did not reveal any particular homologies or subtype-specific sequences. The DNA sequence data also showed that even though the protein coding regions of the histone genes have been conserved exceptionally well throughout evolution, their 5' untranslated regions have not been conserved as well.

• Molecules and Cells
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• v.37 no.10
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• pp.734-741
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• 2014

Histone modifications on major transcription factor target genes are one of the major regulatory mechanisms controlling adipogenesis. Plant homeodomain finger 2 (PHF2) is a Jumonji domain-containing protein and is known to demethylate the histone H3K9, a repressive gene marker. To better understand the function of PHF2 in adipocyte differentiation, we constructed stable PHF2 knock-down cells by using the mouse pre-adipocyte cell line 3T3-L1. When induced with adipogenic media, PHF2 knock-down cells showed reduced lipid accumulation compared to control cells. Differential expression using a cDNA microarray revealed significant reduction of metabolic pathway genes in the PHF2 knock-down cell line after differentiation. The reduced expression of major transcription factors and adipokines was confirmed with reverse transcription- quantitative polymerase chain reaction and Western blotting. We further performed co-immunoprecipitation analysis of PHF2 with four major adipogenic transcription factors, and we found that CCATT/enhancer binding protein (C/EBP)${\alpha}$ and C/EBP${\delta}$ physically interact with PHF2. In addition, PHF2 binding to target gene promoters was confirmed with a chromatin immunoprecipitation experiment. Finally, histone H3K9 methylation markers on the PHF2-binding sequences were increased in PHF2 knock-down cells after differentiation. Together, these results demonstrate that PHF2 histone demethylase controls adipogenic gene expression during differentiation.