Lysine residues in N-terminal and C-terminal regions of human histone H2A are targets for biotinylation by biotinidase

Yap Ching Chew, Gabriela Camporeale, Nagarama Kothapalli, Gautam Sarath, Janos Zempleni

Research output: Contribution to journalArticle

72 Citations (Scopus)

Abstract

In eukaryotic cell nuclei, DNA associates with the core histones H2A, H2B, H3 and H4 to form nucleosomal core particles. DNA binding to histones is regulated by posttranslational modifications of N-terminal tails (e.g., acetylation and methylation of histones). These modifications play important roles in the epigenetic control of chromatin structure. Recently, evidence that biotinidase and holocarboxylase synthetase (HCS) catalyze the covalent binding of biotin to histones has been provided. The primary aim of this study was to identify biotinylation sites in histone H2A and its variant H2AX. Secondary aims were to determine whether acetylation and methylation of histone H2A affect subsequent biotinylation and whether biotinidase and HCS localize to the nucleus in human cells. Biotinylation sites were identified using synthetic peptides as substrates for biotinidase. These studies provided evidence that K9 and K13 in the N-terminus of human histones H2A and H2AX are targets for biotinylation and that K125, K127 and K129 in the C-terminus of histone H2A are targets for biotinylation. Biotinylation of lysine residues was decreased by acetylation of adjacent lysines but was increased by dimethylation of adjacent arginines. The existence of biotinylated histone H2A in vivo was confirmed by using modification-specific antibodies. Antibodies to biotinidase and HCS localized primarily to the nuclear compartment, consistent with a role for these enzymes in regulating chromatin structure. Collectively, these studies have identified five novel biotinylation sites in human histones; histone H2A is unique among histones in that its biotinylation sites include amino acid residues from the C-terminus.

Original languageEnglish (US)
Pages (from-to)225-233
Number of pages9
JournalJournal of Nutritional Biochemistry
Volume17
Issue number4
DOIs
StatePublished - Apr 1 2006

Fingerprint

Biotinidase
Biotinylation
Histones
Lysine
Acetylation
Methylation
Chromatin
Cells
Antibodies
DNA
Eukaryotic Cells
Post Translational Protein Processing
Biotin
Cell Nucleus

Keywords

  • Biocytin
  • Biotin
  • Biotinidase
  • Histone H2A
  • Holocarboxylase synthetase
  • Lysine

ASJC Scopus subject areas

  • Endocrinology, Diabetes and Metabolism
  • Biochemistry
  • Molecular Biology
  • Nutrition and Dietetics
  • Clinical Biochemistry

Cite this

Lysine residues in N-terminal and C-terminal regions of human histone H2A are targets for biotinylation by biotinidase. / Chew, Yap Ching; Camporeale, Gabriela; Kothapalli, Nagarama; Sarath, Gautam; Zempleni, Janos.

In: Journal of Nutritional Biochemistry, Vol. 17, No. 4, 01.04.2006, p. 225-233.

Research output: Contribution to journalArticle

Chew, Yap Ching ; Camporeale, Gabriela ; Kothapalli, Nagarama ; Sarath, Gautam ; Zempleni, Janos. / Lysine residues in N-terminal and C-terminal regions of human histone H2A are targets for biotinylation by biotinidase. In: Journal of Nutritional Biochemistry. 2006 ; Vol. 17, No. 4. pp. 225-233.
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