• 제목/요약/키워드: Histone

검색결과 545건 처리시간 0.022초

Nucleohistone과 DNase 1 과의 相互作用의 Cooperativity 및 이에 미치는 Spermine과 Dansylation 效果 (Cooperativity of the Interaction of Nucleohistone and DNase 1, and Effects of Spermine and Dansylation on It)

  • 이찬용;고동성
    • 대한화학회지
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    • 제29권3호
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    • pp.304-310
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    • 1985
  • 송아지 흉선 nucleohistone의 DNase 1에 對한 susceptibility와 相互作用의 cooperativity에 미치는 spermine의 效果를 nucleostone의 構造變移와 關聯시켜 調査하였다. 이들 data로 부터 nucleohistone은 遊離 DNA와는 對照的으로 spermine에 의하여 monomoclecular condensation을 일으키지 않고 intermolecular aggregation을 이루며 nucleohistone의 DNase 1과의 相互作用 cooperativity가 spermine에 의하여 增加됨을 推理할 수 있다. Nucleohistine의 histone 部分의 cooperativity에 關한 機能的 役割을 究明하기 위하여 histone 部分을 단실化시킨 DNS-nucleohistone을 製造하여 DNase 1 과의 相互作用을 調査하여 보았는바 negative cooperativity로 나타났다. 이로 부터 nucleohistone의 histone部分은 nucleohistone의 cooperativity에 影響을 미치리라고 推理할 수 있다.

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An Isothermal Titration Microcalorimetric Study on the Interaction of Three Water-Soluble Porphyrins with Histone H2B

  • Bordbar, A.K.;Ghaderi, A.R.;Safaei, E.;Tangestaninejad, S.;Eslami, A.;Saboury, A.A.;Moosavi Movahedi, A.A.
    • Bulletin of the Korean Chemical Society
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    • 제24권5호
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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.

Identification of histone methyltransferase RE-IIBP target genes in leukemia cell line

  • Son, Hye-Ju;Kim, Ji-Young;Rhee, Sang-Myung;Seo, Sang-Beom
    • Animal cells and systems
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    • 제16권4호
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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.

Novel $\delta$-Lactam base Histone Deacetylase Inhibitors: Synthesis and Biological Evaluation I.

  • Park, Bum-Woo;Ryu, Dong-Kyu;Kim, Tae-Kyun;Park, Song-Kyu;Han, Jeong-Hwan;Han, Gyoon-Hee
    • 대한약학회:학술대회논문집
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    • 대한약학회 2003년도 Proceedings of the Convention of the Pharmaceutical Society of Korea Vol.2-2
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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)

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Histone Modifications During DNA Replication

  • Falbo, Karina B.;Shen, Xuetong
    • Molecules and Cells
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    • 제28권3호
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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.

Expression of Chimeric Chicken-Yeast-Chicken H2B Histone Gene

  • Son, Seung-Yeol
    • Journal of Microbiology and Biotechnology
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    • 제3권3호
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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.

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Histone Deactylase Inhibitors as Novel Target for Cancer, Diabetes, and Inflammation

  • Singh, Parul;Madhavan, Thirumurthy
    • 통합자연과학논문집
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    • 제6권1호
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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.

Cell Cycle Regulated Expression of Subcloned Chicken H3 Histone Genes and Their 5' Flanking Sequences

  • Son, Seung-Yeol;Tae, Gun-Sik
    • Journal of Microbiology and Biotechnology
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    • 제4권4호
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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.

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The Histone Demethylase PHF2 Promotes Fat Cell Differentiation as an Epigenetic Activator of Both C/EBPα and C/EBPδ

  • Lee, Kyoung-Hwa;Ju, Uk-Il;Song, Jung-Yup;Chun, Yang-Sook
    • Molecules and Cells
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    • 제37권10호
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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.