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  1. TI=Biological functions of biotinylated histones
  2. AU="Metko, Alma"
  3. AU="van Kuppenveld, Savannah Ir"

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  1. Artikel: Biological functions of biotinylated histones.

    Kothapalli, Nagarama / Camporeale, Gabriela / Kueh, Alice / Chew, Yap C / Oommen, Anna M / Griffin, Jacob B / Zempleni, Janos

    The Journal of nutritional biochemistry

    2005  Band 16, Heft 7, Seite(n) 446–448

    Abstract: ... to investigate biological functions of histone biotinylation. Evidence was provided that biotinylation ... biotinylation sites in histones H2A, H3 and H4. Biotinylation site-specific antibodies were generated ... Histones H1, H2A, H2B, H3 and H4 are DNA-binding proteins that mediate the folding of DNA ...

    Abstract Histones H1, H2A, H2B, H3 and H4 are DNA-binding proteins that mediate the folding of DNA into chromatin. Various posttranslational modifications of histones regulate processes such as transcription, replication and repair of DNA. Recently, a novel posttranslational modification has been identified: covalent binding of the vitamin biotin to lysine residues in histones, mediated by biotinidase and holocarboxylase synthetase. Here we describe a novel peptide-based technique, which was used to identify eight distinct biotinylation sites in histones H2A, H3 and H4. Biotinylation site-specific antibodies were generated to investigate biological functions of histone biotinylation. Evidence was provided that biotinylation of histones plays a role in cell proliferation, gene silencing and cellular response to DNA damage.
    Mesh-Begriff(e) Animals ; Biotin/metabolism ; Biotinylation ; Chromatin/chemistry ; Chromatin/metabolism ; Enzymes/metabolism ; Histones/metabolism ; Humans
    Chemische Substanzen Chromatin ; Enzymes ; Histones ; Biotin (6SO6U10H04)
    Sprache Englisch
    Erscheinungsdatum 2005-06-27
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, U.S. Gov't, P.H.S. ; Review
    ZDB-ID 1014929-6
    ISSN 1873-4847 ; 0955-2863
    ISSN (online) 1873-4847
    ISSN 0955-2863
    DOI 10.1016/j.jnutbio.2005.03.025
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel: Biological functions of biotinylated histones

    Kothapalli, N / Camporeale, G / Kueh, A / Chew, Y.C / Oommen, A.M / Griffin, J.B / Zempleni, J

    Journal of nutritional biochemistry. 2005 July, v. 16, no. 7

    2005  

    Abstract: ... to investigate biological functions of histone biotinylation. Evidence was provided that biotinylation ... biotinylation sites in histones H2A, H3 and H4. Biotinylation site-specific antibodies were generated ... Histones H1, H2A, H2B, H3 and H4 are DNA-binding proteins that mediate the folding of DNA ...

    Abstract Histones H1, H2A, H2B, H3 and H4 are DNA-binding proteins that mediate the folding of DNA into chromatin. Various posttranslational modifications of histones regulate processes such as transcription, replication and repair of DNA. Recently, a novel posttranslational modification has been identified: covalent binding of the vitamin biotin to lysine residues in histones, mediated by biotinidase and holocarboxylase synthetase. Here we describe a novel peptide-based technique, which was used to identify eight distinct biotinylation sites in histones H2A, H3 and H4. Biotinylation site-specific antibodies were generated to investigate biological functions of histone biotinylation. Evidence was provided that biotinylation of histones plays a role in cell proliferation, gene silencing and cellular response to DNA damage.
    Schlagwörter cell physiology ; biotin ; chromatin ; DNA damage ; epigenetics ; histones ; DNA-binding proteins ; gene silencing ; enzyme activity ; cell proliferation ; nutrition-genotype interaction
    Sprache Englisch
    Erscheinungsverlauf 2005-07
    Umfang p. 446-448.
    Dokumenttyp Artikel
    ZDB-ID 1014929-6
    ISSN 1873-4847 ; 0955-2863
    ISSN (online) 1873-4847
    ISSN 0955-2863
    Datenquelle NAL Katalog (AGRICOLA)

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    Verfügbar in ZB MED Bonn

    Z 5044: Hefte anzeigen

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  3. Buch ; Dissertation / Habilitation: Biological functions of biotinylated histones H3 and H4

    Pestinger, Valerie

    2009  

    Verfasserangabe by Valerie Pestinger
    Sprache Englisch
    Umfang 91 leaves :, ill. ;, 28 cm.
    Dokumenttyp Buch ; Dissertation / Habilitation
    Dissertation / Habilitation Thesis (M.S.)--University of Nebraska--Lincoln, 2009
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  4. Artikel: Histone modifications dictate specific biological readouts.

    Munshi, Anjana / Shafi, Gowhar / Aliya, Nishat / Jyothy, Akka

    Journal of genetics and genomics = Yi chuan xue bao

    2009  Band 36, Heft 2, Seite(n) 75–88

    Abstract: ... twice around an octamer of core histones. The core histones bear a highly dynamic N-terminal amino acid ... In this review, we focus on these complex modification patterns and their biological functions. Moreover ... function of the chromatin fiber. Errors in this histone code may be involved in many human diseases ...

    Abstract The basic unit of chromatin is the nucleosomal core particle, containing 147 bp of DNA that wraps twice around an octamer of core histones. The core histones bear a highly dynamic N-terminal amino acid tail around 20-35 residues in length and rich in basic amino acids. These tails extending from the surface of nucleosome play an important role in folding of nucleosomal arrays into higher order chromatin structure, which plays an important role in eukaryotic gene regulation. The amino terminal tails protruding from the nuclesomes get modified by the addition of small groups such as methyl, acetyl and phosphoryl groups. In this review, we focus on these complex modification patterns and their biological functions. Moreover, these modifications seem to be part of a complex scheme where distinct histone modifications act in a sequential manner or in combination to form a "histone code" read by other proteins to control the structure and/or function of the chromatin fiber. Errors in this histone code may be involved in many human diseases especially cancer, the nature of which could be therapeutically exploited. Increasing evidence suggests that many proteins bear multiple, distinct modifications, and the ability of one modification to antagonize or synergize the deposition of another can have significant biological consequences.
    Mesh-Begriff(e) Acetylation ; Animals ; Biotinylation ; DNA Damage ; Gene Expression Regulation ; Heterochromatin/metabolism ; Histones/genetics ; Histones/metabolism ; Humans ; Methylation ; Protein Processing, Post-Translational ; Ubiquitination
    Chemische Substanzen Heterochromatin ; Histones
    Sprache Englisch
    Erscheinungsdatum 2009-02
    Erscheinungsland China
    Dokumenttyp Journal Article ; Review
    ZDB-ID 2374568-X
    ISSN 1873-5533 ; 1673-8527
    ISSN (online) 1873-5533
    ISSN 1673-8527
    DOI 10.1016/S1673-8527(08)60094-6
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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