Regulation of DNA primase activity by phosphorylation of histone-H1 in regenerating rat liver.
The biological importance of histone H1 was investigated in relation to the cell cycle using liver regeneration in rat. Histone H1 was extracted from the regenerating rat liver at various intervals after partial hepatectomy and the number of phosphate residues was measured. The inhibitory effect of the extracted histone H1 on DNA primase was assayed. The activities of DNA polymerase-alpha, DNA primase and DNA synthesis were also determined in the regenerating rat liver. It was found that: 1) phosphate residue in histone H1 from normal rat liver was between 2-3 mol/mol of histone H1. 2) The number of phosphate residues did not change for the first 16h after partial hepatectomy. 3) A dramatic sudden increase of phosphate residues was detected at 18h after partial hepatectomy. 4) The high levels of phosphate residues remained constant thereafter up to 50h. 5) DNA primase activity was less inhibited by highly phosphorylated than by slightly phosphorylated histone H1. It seems probable that phosphorylation of histone H1 is needed for the releasing of DNA primase activity from its inhibited state, which would start DNA synthesis together with DNA polymerase-alpha.
Takada
S
S
Department of Biochemistry, School of Medicine, Tokai University, Isehara-shi, Japan.
Magira
T
T
Suzuki
E
E
Yamamura
M
M
D000818:Animals; D019915:DNA Primase; D006498:Hepatectomy; D006657:Histones / Q000378:metabolism*; D008115:Liver Regeneration / Q000502:physiology*; D010766:Phosphorylation; D012316:RNA Nucleotidyltransferases / Q000378:metabolism*; D051381:Rats
D006657:Histones; D019915:DNA Primase; D012316:RNA Nucleotidyltransferases