Alteration of DNA primase activity by phosphorylation and de-phosphorylation of histone H1.
To investigate the effect of histone H1 on DNA primase activity, partially purified DNA primase from mouse FM3A cells was used. It was found that histone H1 dose dependently inhibited DNA primase. Interestingly phosphorylation of histone H1 reduced the inhibitory activity of the histone. However, de-phosphorylation of the phosphorylated histone H1 resumed the inhibitory activity of DNA primase. These findings lead us to the assumption that phosphorylation and de-phosphorylation of histone may regulate the cell cycle by controlling DNA synthesis through reverse inhibition of DNA primase.
Takada
S
S
Department of Biochemistry, School of Medicine, Tokai University, Kanagawa, Japan.
Magira
T
T
Yamamura
M
M
D000818:Animals; D002417:Cattle; D019915:DNA Primase; D004261:DNA Replication / Q000187:drug effects; D006657:Histones / Q000378:metabolism* / Q000494:pharmacology; D051379:Mice; D010766:Phosphorylation; D012316:RNA Nucleotidyltransferases / Q000037:antagonists & inhibitors* / Q000494:pharmacology
D006657:Histones; D019915:DNA Primase; D012316:RNA Nucleotidyltransferases