Biotinylation of histones in human cells. Effects of cell proliferation.
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.
Stanley
J S
JS
Department of Pediatrics, Division of Immunology and Allergy, University of Arkansas for Medical Sciences and Arkansas Children's Hospital Research Institute, Little Rock, USA.
Griffin
J B
JB
Zempleni
J
J
D000581:Amidohydrolases / Q000235:genetics / Q000378:metabolism; D001710:Biotin / Q000378:metabolism; D043523:Biotinidase; D019921:Biotinylation; D002453:Cell Cycle; D002455:Cell Division; D002467:Cell Nucleus / Q000737:chemistry / Q000378:metabolism; D002478:Cells, Cultured; D015870:Gene Expression; D006657:Histones / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D007963:Leukocytes, Mononuclear / Q000166:cytology / Q000201:enzymology / Q000378:metabolism; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism
D006657:Histones; D012333:RNA, Messenger; D001710:Biotin; D000581:Amidohydrolases; D043523:Biotinidase