• Title/Summary/Keyword: Histone (H₂B)

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Expression of Chimeric Chicken-Yeast-Chicken H2B Histone Gene

  • Son, Seung-Yeol
    • 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.

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Histone H4-Specific Deacetylation at Active Coding Regions by Hda1C

  • Lee, Min Kyung;Kim, TaeSoo
    • Molecules and Cells
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    • v.43 no.10
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    • pp.841-847
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    • 2020
  • Histone acetylation and deacetylation play central roles in the regulation of chromatin structure and transcription by RNA polymerase II (RNA Pol II). Although Hda1 histone deacetylase complex (Hda1C) is known to selectively deacetylate histone H3 and H2B to repress transcription, previous studies have suggested its potential roles in histone H4 deacetylation. Recently, we have shown that Hda1C has two distinct functions in histone deacetylation and transcription. Histone H4-specific deacetylation at highly transcribed genes negatively regulates RNA Pol II elongation and H3 deacetylation at inactive genes fine-tunes the kinetics of gene induction upon environmental changes. Here, we review the recent understandings of transcriptional regulation via histone deacetylation by Hda1C. In addition, we discuss the potential mechanisms for histone substrate switching by Hda1C, depending on transcriptional frequency and activity.

Studies on the Histones of the Genus Rhizopus (Rhizopus속의 histones에 관한 연구)

  • 민병례;이은영
    • Korean Journal of Microbiology
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    • v.28 no.2
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    • pp.128-133
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    • 1990
  • The chromatin of all higher eukaryotic cells contains a group of very basic low-mole-cular weight proteins, the histones. But much less is known about histones in lower eukaryotes. Our purpose was to study the histones of the genus Rhizopus. After isolation and purification of nucleoprotein the basic nucleoproteins were analyzed by gel electrophoresis, in sodium dodecyl sulfate as well as acid/urea gels and compared with calf thymus histones. Their electrophoretic mobility in polyacrylamide gel indicate that they are histone homologous, although not identical, to the H2A, H2B, H3 and H4 histones of mammals with the exception of H1. The result suggests that Rhizopus thus appears to contain histone proteins which are homologous to the histones from in higher eukaryotes. The similarity between the calf thymus histone H1 and the Rhizopus high band group remains to be discussed.

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Histone H4 is cleaved by granzyme A during staurosporine-induced cell death in B-lymphoid Raji cells

  • Lee, Phil Young;Park, Byoung Chul;Chi, Seung Wook;Bae, Kwang-Hee;Kim, Sunhong;Cho, Sayeon;Kang, Seongman;Kim, Jeong-Hoon;Park, Sung Goo
    • BMB Reports
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    • v.49 no.10
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    • pp.560-565
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    • 2016
  • Granzyme A (GzmA) was first identified as a cytotoxic T lymphocyte protease protein with limited tissue expression. A number of cellular proteins are known to be cleaved by GzmA, and its function is to induce apoptosis. Histones H1, H2B, and H3 were identified as GzmA substrates during apoptotic cell death. Here, we demonstrated that histone H4 was cleaved by GzmA during staurosporine-induced cell death; however, in the presence of caspase inhibitors, staurosporine-treated Raji cells underwent necroptosis instead of apoptosis. Furthermore, histone H4 cleavage was blocked by the GzmA inhibitor nafamostat mesylate and by GzmA knockdown using siRNA. These results suggest that histone H4 is a novel substrate for GzmA in staurosporine-induced cells.

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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    • 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.

Characterization of histone gene expression in sevenband grouper, Hyporthodus septemfasciatus against nervous necrosis virus infection

  • Lee, Dong-Ryun;Lee, A-Reum;Krishnan, Rahul;Jang, Yo-Seb;Oh, Myung-Joo;Kim, Jong-Oh
    • Journal of fish pathology
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    • v.35 no.1
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    • pp.121-128
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    • 2022
  • Recent studies revealed that histone proteins are involved in innate immune responses during pathogen invasion as well as DNA packing. This study characterized the histone genes (H2A.V) of sevenband groupers and analyzed gene expression in NNV-infected sevenband groupers. The open reading frame (ORF) of H2A.V is 387 bp which encoded 128 amino acid residues. The deduced amino acid sequence of H2A.V harbor a highly conserved domain for H2A/H2B/H3 and H2A_C binding domain. Quantitative real-time PCR analysis showed that H2A.V had a high gene expression level in the brain and blood after being NNV-infected. An increase in extracellular histone protein in the blood has been identified as a biomarker for vascular function in humans. More research is required to understand histone's immune response at the protein level or in aquatic animals.

The PcG protein hPc2 interacts with the N-terminus of histone demethylase JARID1B and acts as a transcriptional co-repressor

  • Zhou, Wu;Chen, Haixiang;Zhang, Lihuang
    • BMB Reports
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    • v.42 no.3
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    • pp.154-159
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    • 2009
  • JARID1B (jumonji AT rich interactive domain 1B) is a large nuclear protein that is highly expressed in breast cancers and is proposed to function as a repressor of gene expression. In this paper, a phage display screen using the N-terminus of JARID1B as bait identified one of the JARID1B interacting proteins, namely PcG protein (Polycomb group) hPc2. We demonstrated that the C-terminal region, including the COOH box, was required for the interaction with the N-terminus of JARID1B. In a reporter assay system, co-expression of JARID1B with hPc2 significantly enhanced the transcriptional repression. These results support a role for hPc2 acting as a transcriptional co-repressor.

Histone H3 is Digested by Granzyme A During Compromised Cell Death in the Raji Cells

  • Lee, Phil Young;Park, Byoung Chul;Chi, Seung Wook;Bae, Kwang-Hee;Kim, Sunhong;Cho, Sayeon;Kim, Jeong-Hoon;Park, Sung Goo
    • Journal of Microbiology and Biotechnology
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    • v.25 no.9
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    • pp.1578-1582
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    • 2015
  • Granzyme A (GzmA) was identified as a cytotoxic T lymphocyte protease protein expressed in the nucleus. A number of nuclear proteins are well known as GzmA substrates, and GzmA is related with caspase-independent apoptosis. Histones H1, H2B, and H3 were identified as GzmA substrates through in vitro experiment with purified nucleosome. Here, we demonstrated that histone H3 was cleaved by GzmA in vivo during staurosporine-induced cell death. Moreover, histone H3 cleavage was blocked by the GzmA inhibitor nafamostat mesylate and by GzmA knockdown using siRNA. Taken together, we verified that histone H3 is a real substrate for GzmA in vivo in the Raji cells treated by staurosporin.

Cloning of the Setd1b gene of Mus musculus, a novel histone methyl transferase target in the epigenetic therapy of cancers

  • Morishita, Masayo;Cho, Minju;Ryu, Juhee;Mevius, Damiaan E.H.F.;Di Luccio, Eric
    • Current Research on Agriculture and Life Sciences
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    • v.28
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    • pp.63-68
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    • 2010
  • The epigenetic therapy of cancers is emerging as an effective and valuable approach to both chemotherapy and the chemoprevention of cancer. The utilization of epigenetic targets that include histone methyltransferase (HMTase), Histone deacetylatase, and DNA methyltransferase, are emerging as key therapeutic targets. SET containing proteins such as the HMTase Setd1b has been found significantly amplified in cancerous cells. In order to shed some light on the histone methyl transferase family, we cloned the Setd1b gene from Mus musculus and build a collection of vectors for recombinant protein expression in E.coli that will pave the way for further structural biology studies. We prospect the role of the Setd1b pathway in cancer therapy and detail its unique value for designing novel anti-cancer epigenetic-drugs.

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Global Histone H4 Acetylation of IGF1 and GH Genes in Lungs of Somatic Cell Cloned Calves

  • Zhang, L.;Wang, S.H.;Fan, B.L.;Dai, Y.P.;Fei, J.;Li, N.
    • Asian-Australasian Journal of Animal Sciences
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    • v.19 no.8
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    • pp.1090-1094
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    • 2006
  • Histone acetylation modification is one key mechanism in the regulation of gene activation. In this study, we investigated the global levels of histone H4 acetylation of insulin like growth factor I (IGF1) and growth hormone (GH) genes in the lungs of two somatic cell cloned calves. Data showed the levels of histone H4 acetylation of IGF1 and GH genes vary widely within different gene regions, and, in almost all regions of the two genes, acetylation levels are lower in the aberrant clone than in the normal clone. Thus we suggest that inefficient epigenetic reprogramming in the clone may affect the balance between acetylation and deacetylation, which will affect normal growth and development. These findings will also have implications for improvement of cloning success rates.