Biotinylation of histones in human cells

Effects of cell proliferation

J. Steven Stanley, Jacob B. Griffin, Janos Zempleni

Research output: Contribution to journalArticle

131 Citations (Scopus)

Abstract

An enzymatic mechanism has been proposed by which biotinidase may catalyze biotinylation of histones. Here, human cells were found to covalently bind biotin to histones H1, H2A, H2B, H3, and H4. Cells respond to proliferation with increased biotinylation of histones; biotinylation increases early in the cell cycle and remains increased during the cycle. Notwithstanding the catalytic role of biotinidase in biotinylation of histones, mRNA encoding biotinidase and biotinidase activity did not parallel the increased biotinylation of histones in proliferating cells. Biotinylation of histones might be regulated by enzymes other than biotinidase or by the rate of histone debiotinylation.

Original languageEnglish (US)
Pages (from-to)5424-5429
Number of pages6
JournalEuropean Journal of Biochemistry
Volume268
Issue number20
DOIs
StatePublished - Oct 20 2001

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Biotinylation
Biotinidase
Cell proliferation
Histones
Cells
Cell Proliferation
Biotin
Cell Cycle
Messenger RNA
Enzymes

Keywords

  • Biotin
  • Biotinidase
  • Cell proliferation
  • Histones

ASJC Scopus subject areas

  • Biochemistry

Cite this

Biotinylation of histones in human cells : Effects of cell proliferation. / Steven Stanley, J.; Griffin, Jacob B.; Zempleni, Janos.

In: European Journal of Biochemistry, Vol. 268, No. 20, 20.10.2001, p. 5424-5429.

Research output: Contribution to journalArticle

Steven Stanley, J. ; Griffin, Jacob B. ; Zempleni, Janos. / Biotinylation of histones in human cells : Effects of cell proliferation. In: European Journal of Biochemistry. 2001 ; Vol. 268, No. 20. pp. 5424-5429.
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