Prokaryotic bira ligase biotinylates K4, K9, K18 and K23 in histone H3

Keyna Kobza, Gautam Sarath, Janos Zempleni

Research output: Contribution to journalArticlepeer-review

39 Scopus citations

Abstract

BirA ligase is a prokaryotic ortholog of holocarboxylase synthetase (HCS) that can biotinylate proteins. This study tested the hypothesis that BirA ligase catalyzes the biotinylation of eukaryotic histones. If so, this would mean that recombinant BirA ligase is a useful surrogate for HCS in studies of histone biotinylation. The biological activity of recombinant BirA ligase was confirmed by enzymatic biotinylation of p67. In particular, it was found that BirA ligase biotinylated both calf thymus histone H1 and human bulk histone extracts. Incubation of recombinant BirA ligase with H3-based synthetic peptides showed that lysines 4, 9, 18, and 23 in histone H3 are the targets for the biotinylation by BirA ligase. Modification of the peptides (e.g., serine phosphorylation) affected the subsequent biotinylation by BirA ligase, suggesting crosstalk between modifications. In conclusion, this study suggests that prokaryotic BirA ligase is a promiscuous enzyme and biotinylates eukaryotic histones. Moreover the biotinylation of histones by BirA ligase is consistent with the proposed role of human HCS in chromatin.

Original languageEnglish (US)
Pages (from-to)310-315
Number of pages6
JournalBMB Reports
Volume41
Issue number4
DOIs
StatePublished - 2008

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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