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.
aDepartment of Nutrition and Health Sciences, University of Nebraska at Lincoln, Lincoln, NE 68583-0806, USA
bDepartments of Animal Science and Biochemistry, University of Nebraska at Lincoln, Lincoln, NE 68583-0806, USA
Corresponding 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.
☆ 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).
ABSTRACT