Biotinylation of histones in human cells. Effects of cell proliferation

Eur J Biochem. 2001 Oct;268(20):5424-9. doi: 10.1046/j.0014-2956.2001.02481.x.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amidohydrolases / genetics
  • Amidohydrolases / metabolism
  • Biotin / metabolism
  • Biotinidase
  • Biotinylation*
  • Cell Cycle
  • Cell Division
  • Cell Nucleus / chemistry
  • Cell Nucleus / metabolism
  • Cells, Cultured
  • Gene Expression
  • Histones / isolation & purification
  • Histones / metabolism*
  • Humans
  • Leukocytes, Mononuclear / cytology
  • Leukocytes, Mononuclear / enzymology
  • Leukocytes, Mononuclear / metabolism
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism

Substances

  • Histones
  • RNA, Messenger
  • Biotin
  • Amidohydrolases
  • Biotinidase