The Journal of Nutritional Biochemistry
Volume 16, Issue 7 , Pages 446-448, July 2005

Biological functions of biotinylated histones☆

  • Nagarama Kothapalli

      Affiliations

    • Department of Nutrition and Health Sciences, University of Nebraska at Lincoln, Lincoln, NE 68583-0806, USA
    • ,
  • Gabriela Camporeale

      Affiliations

    • Department of Nutrition and Health Sciences, University of Nebraska at Lincoln, Lincoln, NE 68583-0806, USA
    • ,
  • Alice Kueh

      Affiliations

    • Department of Nutrition and Health Sciences, University of Nebraska at Lincoln, Lincoln, NE 68583-0806, USA
    • ,
  • Yap C. Chew

      Affiliations

    • Department of Nutrition and Health Sciences, University of Nebraska at Lincoln, Lincoln, NE 68583-0806, USA
    • ,
  • Anna M. Oommen

      Affiliations

    • Department of Nutrition and Health Sciences, University of Nebraska at Lincoln, Lincoln, NE 68583-0806, USA
    • ,
  • Jacob B. Griffin

      Affiliations

    • Department of Nutrition and Health Sciences, University of Nebraska at Lincoln, Lincoln, NE 68583-0806, USA
    • ,
  • Janos Zempleni

      Affiliations

    • Department of Nutrition and Health Sciences, University of Nebraska at Lincoln, Lincoln, NE 68583-0806, USA
    • Departments of Animal Science and Biochemistry, University of Nebraska at Lincoln, Lincoln, NE 68583-0806, USA
    • Corresponding Author InformationCorresponding author. Department of Nutrition and Health Sciences, University of Nebraska at Lincoln, Lincoln, NE 68583-0806, USA. Tel.: +1 402 472 3270; fax: +1 402 472 1587.

Received 30 March 2005; received in revised form 30 March 2005; accepted 30 March 2005.

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.

Keywords: Biotin, Chromatin, DNA damage, Epigenetics, Histones, Human

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☆ This paper was presented at the “International Symposium: Vitamins as Regulators of Genetic Expression: Biotin as a Model” NAFTA Satellite Meeting to the XXV National Congress of Biochemistry held December 3–4, 2004, in Ixtapa, Zihuatanejo, Mexico. This meeting was sponsored by Sociedad Mexicana de Bioquimica A.C.; Programa de Doctorado en Ciencias Biomedicas, Universidad Nacional Autonoma de Mexico; Laboratorios Roche-Syntex, Mexico; and Instituto de Investigaciones Biomedicas, Universidad Nacional Autonoma de Mexico. This paper is a contribution of the University of Nebraska Agricultural Research Division, Lincoln, NE 68583, USA (Journal Series No. 14855).

PII: S0955-2863(05)00098-7

doi:10.1016/j.jnutbio.2005.03.025

The Journal of Nutritional Biochemistry
Volume 16, Issue 7 , Pages 446-448, July 2005

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