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  1. Article ; Online: MeCP2 is the protector of epigenome integrity, membrane-less nuclear architecture, and stability of chromatin assembly.

    Rastegar, Mojgan / Davie, James R

    Epigenomics

    2023  Volume 15, Issue 20, Page(s) 1027–1031

    Abstract: Tweetable abstract MeCP2 is an epigenetic factor with global impact in epigenome integrity, membrane-less nuclear architecture, and chromatin stability. Our Editorial covers recent advances on these important topics. ...

    Abstract Tweetable abstract MeCP2 is an epigenetic factor with global impact in epigenome integrity, membrane-less nuclear architecture, and chromatin stability. Our Editorial covers recent advances on these important topics.
    MeSH term(s) Humans ; Chromatin/genetics ; Chromatin Assembly and Disassembly ; DNA Methylation ; Epigenome ; Epigenomics ; Methyl-CpG-Binding Protein 2/genetics ; Methyl-CpG-Binding Protein 2/metabolism
    Chemical Substances Chromatin ; Methyl-CpG-Binding Protein 2
    Language English
    Publishing date 2023-11-08
    Publishing country England
    Document type Editorial
    ZDB-ID 2537199-X
    ISSN 1750-192X ; 1750-1911
    ISSN (online) 1750-192X
    ISSN 1750-1911
    DOI 10.2217/epi-2023-0310
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Broad histone H4 monomethylation marks expressed genes involved in translation.

    Fatemiyan, Narges / Davie, James R

    Genome

    2023  Volume 66, Issue 8, Page(s) 224–234

    Abstract: H4K20me1 (histone H4 monomethylated at lysine 20) generally has a broad distribution along genes and has been reported to be associated with expressed and repressed genes. In contrast, H3K4me3 (histone H3 trimethylated at lysine 4) is positioned as a ... ...

    Abstract H4K20me1 (histone H4 monomethylated at lysine 20) generally has a broad distribution along genes and has been reported to be associated with expressed and repressed genes. In contrast, H3K4me3 (histone H3 trimethylated at lysine 4) is positioned as a narrow peak at the 5' end of most expressed genes in vertebrate cells. A small population of genes involved in cell identity has H3K4me3 distributed throughout the gene body. In this report, we show that H4K20me1 is associated with expressed genes in estrogen receptor-positive breast cancer MCF7 cells and erythroleukemic K562 cells. Further, we identified the genes with the broadest H4K20me1 domains in these two cell types. The broad H4K20me1 domain marked gene bodies of expressed genes, but not the promoter or enhancer regions. The most significant GO term (biological processes) of these genes was cytoplasmic translation. There was little overlap between the genes marked with the broad H4K20me1 domain and those marked with H3K4me3. H4K20me1 and H3K79me2 distributions along expressed gene bodies were similar, suggesting a relationship between the enzymes catalyzing these histone modifications.
    MeSH term(s) Histones/genetics ; Histones/metabolism ; Lysine/metabolism
    Chemical Substances Histones ; Lysine (K3Z4F929H6)
    Language English
    Publishing date 2023-05-08
    Publishing country Canada
    Document type Journal Article
    ZDB-ID 639031-6
    ISSN 1480-3321 ; 0831-2796
    ISSN (online) 1480-3321
    ISSN 0831-2796
    DOI 10.1139/gen-2023-0011
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Chicken Erythrocyte: Epigenomic Regulation of Gene Activity.

    Beacon, Tasnim H / Davie, James R

    International journal of molecular sciences

    2023  Volume 24, Issue 9

    Abstract: The chicken genome is one-third the size of the human genome and has a similarity of sixty percent when it comes to gene content. Harboring similar genome sequences, chickens' gene arrangement is closer to the human genomic organization than it is to ... ...

    Abstract The chicken genome is one-third the size of the human genome and has a similarity of sixty percent when it comes to gene content. Harboring similar genome sequences, chickens' gene arrangement is closer to the human genomic organization than it is to rodents. Chickens have been used as model organisms to study evolution, epigenome, and diseases. The chicken nucleated erythrocyte's physiological function is to carry oxygen to the tissues and remove carbon dioxide. The erythrocyte also supports the innate immune response in protecting the chicken from pathogens. Among the highly studied aspects in the field of epigenetics are modifications of DNA, histones, and their variants. In understanding the organization of transcriptionally active chromatin, studies on the chicken nucleated erythrocyte have been important. Through the application of a variety of epigenomic approaches, we and others have determined the chromatin structure of expressed/poised genes involved in the physiological functions of the erythrocyte. As the chicken erythrocyte has a nucleus and is readily isolated from the animal, the chicken erythrocyte epigenome has been studied as a biomarker of an animal's long-term exposure to stress. In this review, epigenomic features that allow erythroid gene expression in a highly repressive chromatin background are presented.
    MeSH term(s) Humans ; Animals ; Chickens/genetics ; Chickens/metabolism ; Epigenomics ; Chromatin/genetics ; Histones/genetics ; Histones/metabolism ; Erythrocytes/metabolism
    Chemical Substances Chromatin ; Histones
    Language English
    Publishing date 2023-05-05
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms24098287
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Transcriptionally Active Chromatin-Lessons Learned from the Chicken Erythrocyte Chromatin Fractionation.

    Beacon, Tasnim H / Davie, James R

    Cells

    2021  Volume 10, Issue 6

    Abstract: ... Several seminal features of transcriptionally active chromatin were discovered in this system. Davie and ...

    Abstract The chicken erythrocyte model system has been valuable to the study of chromatin structure and function, specifically for genes involved in oxygen transport and the innate immune response. Several seminal features of transcriptionally active chromatin were discovered in this system. Davie and colleagues capitalized on the unique features of the chicken erythrocyte to separate and isolate transcriptionally active chromatin and silenced chromatin, using a powerful native fractionation procedure. Histone modifications, histone variants, atypical nucleosomes (U-shaped nucleosomes) and other chromatin structural features (open chromatin) were identified in these studies. More recently, the transcriptionally active chromosomal domains in the chicken erythrocyte genome were mapped by combining this chromatin fractionation method with next-generation DNA and RNA sequencing. The landscape of histone modifications relative to chromatin structural features in the chicken erythrocyte genome was reported in detail, including the first ever mapping of histone H4 asymmetrically dimethylated at Arg 3 (H4R3me2a) and histone H3 symmetrically dimethylated at Arg 2 (H3R2me2s), which are products of protein arginine methyltransferases (PRMTs) 1 and 5, respectively. PRMT1 is important in the establishment and maintenance of chicken erythrocyte transcriptionally active chromatin.
    MeSH term(s) Animals ; Chickens ; Chromatin/metabolism ; Dose Fractionation, Radiation ; Erythrocytes/metabolism ; Histone Code/physiology ; Histones/metabolism ; Humans ; Methyltransferases/metabolism
    Chemical Substances Chromatin ; Histones ; Methyltransferases (EC 2.1.1.-)
    Language English
    Publishing date 2021-05-30
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2661518-6
    ISSN 2073-4409 ; 2073-4409
    ISSN (online) 2073-4409
    ISSN 2073-4409
    DOI 10.3390/cells10061354
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: The chicken model organism for epigenomic research.

    Beacon, Tasnim H / Davie, James R

    Genome

    2020  Volume 64, Issue 4, Page(s) 476–489

    Abstract: The chicken model organism has advanced the areas of developmental biology, virology, immunology, oncology, epigenetic regulation of gene expression, conservation biology, and genomics of domestication. Further, the chicken model organism has aided in ... ...

    Abstract The chicken model organism has advanced the areas of developmental biology, virology, immunology, oncology, epigenetic regulation of gene expression, conservation biology, and genomics of domestication. Further, the chicken model organism has aided in our understanding of human disease. Through the recent advances in high-throughput sequencing and bioinformatic tools, researchers have successfully identified sequences in the chicken genome that have human orthologs, improving mammalian genome annotation. In this review, we highlight the importance of chicken as an animal model in basic and pre-clinical research. We will present the importance of chicken in poultry epigenetics and in genomic studies that trace back to their ancestor, the last link between human and chicken in the tree of life. There are still many genes of unknown function in the chicken genome yet to be characterized. By taking advantage of recent sequencing technologies, it is possible to gain further insight into the chicken epigenome.
    MeSH term(s) Animals ; Chickens/genetics ; Chromatin/chemistry ; Computational Biology ; Epigenesis, Genetic ; Epigenome ; Epigenomics/methods ; Erythrocytes ; Erythropoiesis ; Gene Expression ; Genetic Techniques ; Genome ; Genomics ; Globins ; High-Throughput Nucleotide Sequencing ; Humans ; Immunity, Innate ; Poultry/genetics ; RNA, Untranslated
    Chemical Substances Chromatin ; RNA, Untranslated ; Globins (9004-22-2)
    Language English
    Publishing date 2020-11-24
    Publishing country Canada
    Document type Journal Article ; Review
    ZDB-ID 639031-6
    ISSN 1480-3321 ; 0831-2796
    ISSN (online) 1480-3321
    ISSN 0831-2796
    DOI 10.1139/gen-2020-0129
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: The Chromatin Structure at the

    Shevkoplyas, Danilo / Vuu, Yen My / Davie, James R / Rastegar, Mojgan

    International journal of molecular sciences

    2022  Volume 23, Issue 24

    Abstract: Methyl CpG binding protein 2 (MeCP2) is an epigenetic reader that binds to methylated CpG dinucleotides and regulates gene transcription. ...

    Abstract Methyl CpG binding protein 2 (MeCP2) is an epigenetic reader that binds to methylated CpG dinucleotides and regulates gene transcription.
    Language English
    Publishing date 2022-12-09
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms232415643
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  7. Article ; Online: Introduction: Genome Biology.

    Beacon, Tasnim H / Davie, James R / Hendzel, Michael J

    Genome

    2021  Volume 64, Issue 4, Page(s) v–vii

    MeSH term(s) Animals ; Biology ; COVID-19/genetics ; Computational Biology ; Disease/genetics ; Epigenomics ; Female ; Genome ; Humans ; Male
    Language English
    Publishing date 2021-04-11
    Publishing country Canada
    Document type Journal Article
    ZDB-ID 639031-6
    ISSN 1480-3321 ; 0831-2796
    ISSN (online) 1480-3321
    ISSN 0831-2796
    DOI 10.1139/gen-2021-0003
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Histone H4 asymmetrically dimethylated at arginine 3 (H4R3me2a), a mark of super-enhancers.

    Sudhakar, Sadhana R N / Wu, Li / Patel, Shrinal / Zovoilis, Athanasios / Davie, James R

    Biochemistry and cell biology = Biochimie et biologie cellulaire

    2023  Volume 102, Issue 2, Page(s) 145–158

    Abstract: Histone H4 asymmetrically dimethylated at arginine 3 (H4R3me2a) is an active histone mark catalyzed by protein arginine methyltransferase 1 (PRMT1), a major arginine methyltransferase in vertebrates catalyzing asymmetric dimethylation of arginine. ... ...

    Abstract Histone H4 asymmetrically dimethylated at arginine 3 (H4R3me2a) is an active histone mark catalyzed by protein arginine methyltransferase 1 (PRMT1), a major arginine methyltransferase in vertebrates catalyzing asymmetric dimethylation of arginine. H4R3me2a stimulates the activity of lysine acetyltransferases such as CBP/p300, which catalyze the acetylation of H3K27, a mark of active enhancers, super-enhancers, and promoters. There are a few studies on the genomic location of H4R3me2a. In chicken polychromatic erythrocytes, H4R3me2a is found in introns and intergenic regions and binds to the globin locus control region (a super-enhancer) and globin regulatory regions. In this report, we analyzed chromatin immunoprecipitation sequencing data for the genomic location of H4R3me2a in the breast cancer cell line MCF7. As in avian cells, MCF7 H4R3me2a is present in intronic and intergenic regions. Nucleosomes with H4R3me2a and H3K27ac next to nucleosome-free regions are found at super-enhancers, enhancers, and promoter regions of expressed genes. Genes with critical roles in breast cancer cells have broad domains of nucleosomes with H4R3me2a, H3K27ac, and H3K4me3. Our results are consistent with PRMT1-mediated H4R3me2a playing a key role in the chromatin organization of regulatory regions of vertebrate genomes.
    MeSH term(s) Animals ; Histones/genetics ; Histones/metabolism ; Nucleosomes ; Arginine/genetics ; DNA, Intergenic ; Globins/genetics ; Globins/metabolism ; Chromatin ; Acetylation
    Chemical Substances Histones ; Nucleosomes ; Arginine (94ZLA3W45F) ; DNA, Intergenic ; Globins (9004-22-2) ; Chromatin
    Language English
    Publishing date 2023-11-27
    Publishing country Canada
    Document type Journal Article
    ZDB-ID 54104-7
    ISSN 1208-6002 ; 0829-8211
    ISSN (online) 1208-6002
    ISSN 0829-8211
    DOI 10.1139/bcb-2023-0211
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Mitogen- and stress-activated protein kinase (MSK1/2) regulated gene expression in normal and disease states.

    Sattarifard, Hedieh / Safaei, Akram / Khazeeva, Enzhe / Rastegar, Mojgan / Davie, James R

    Biochemistry and cell biology = Biochimie et biologie cellulaire

    2023  Volume 101, Issue 3, Page(s) 204–219

    Abstract: The mitogen- and stress-activated protein kinases (MSK) are epigenetic modifiers that regulate gene expression in normal and disease cell states. MSK1 and 2 are involved in a chain of signal transduction events bringing signals from the external ... ...

    Abstract The mitogen- and stress-activated protein kinases (MSK) are epigenetic modifiers that regulate gene expression in normal and disease cell states. MSK1 and 2 are involved in a chain of signal transduction events bringing signals from the external environment of a cell to specific sites in the genome. MSK1/2 phosphorylate histone H3 at multiple sites, resulting in chromatin remodeling at regulatory elements of target genes and the induction of gene expression. Several transcription factors (RELA of NF-κB and CREB) are also phosphorylated by MSK1/2 and contribute to induction of gene expression. In response to signal transduction pathways, MSK1/2 can stimulate genes involved in cell proliferation, inflammation, innate immunity, neuronal function, and neoplastic transformation. Abrogation of the MSK-involved signaling pathway is among the mechanisms by which pathogenic bacteria subdue the host's innate immunity. Depending on the signal transduction pathways in play and the MSK-targeted genes, MSK may promote or hinder metastasis. Thus, depending on the type of cancer and genes involved, MSK overexpression may be a good or poor prognostic factor. In this review, we focus on mechanisms by which MSK1/2 regulate gene expression, and recent studies on their roles in normal and diseased cells.
    MeSH term(s) Gene Expression ; Histones/metabolism ; Mitogens ; Phosphorylation ; Protein Kinases/metabolism ; Humans ; Animals
    Chemical Substances Histones ; Mitogens ; Protein Kinases (EC 2.7.-) ; mitogen and stress-activated protein kinase 1 (EC 2.7.11.1) ; RPS6KA4 protein, human (EC 2.7.11.1)
    Language English
    Publishing date 2023-02-22
    Publishing country Canada
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 54104-7
    ISSN 1208-6002 ; 0829-8211
    ISSN (online) 1208-6002
    ISSN 0829-8211
    DOI 10.1139/bcb-2022-0371
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Epigenetic regulation of ACE2, the receptor of the SARS-CoV-2 virus

    Beacon, Tasnim H / Delcuve, Geneviève P / Davie, James R

    Genome

    2020  Volume 64, Issue 4, Page(s) 386–399

    Abstract: The angiotensin-converting enzyme 2 (ACE2) is the receptor for the three coronaviruses HCoV-NL63, SARS-CoV, and SARS-CoV-2. ACE2 is involved in the regulation of the renin-angiotensin system and blood pressure. ACE2 is also involved in the regulation of ... ...

    Abstract The angiotensin-converting enzyme 2 (ACE2) is the receptor for the three coronaviruses HCoV-NL63, SARS-CoV, and SARS-CoV-2. ACE2 is involved in the regulation of the renin-angiotensin system and blood pressure. ACE2 is also involved in the regulation of several signaling pathways, including integrin signaling.
    MeSH term(s) Angiotensin-Converting Enzyme 2/genetics ; COVID-19 ; Epigenesis, Genetic ; Gene Expression Regulation ; Humans ; Promoter Regions, Genetic ; Protein Processing, Post-Translational ; Receptors, Virus/genetics ; Renin-Angiotensin System ; SARS-CoV-2 ; Signal Transduction
    Chemical Substances Receptors, Virus ; ACE2 protein, human (EC 3.4.17.23) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
    Keywords covid19
    Language English
    Publishing date 2020-10-21
    Publishing country Canada
    Document type Journal Article ; Review
    ZDB-ID 639031-6
    ISSN 1480-3321 ; 0831-2796
    ISSN (online) 1480-3321
    ISSN 0831-2796
    DOI 10.1139/gen-2020-0124
    Database MEDical Literature Analysis and Retrieval System OnLINE

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