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- W1540521703 abstract "The biosynthesis and phosphorylation of histone fractions were measured in synchronized CHO Chinese hamster cells arrested in late G1 by hydroxyurea treatment. Hydroxyurea was found to inhibit the initiation of both DNA and histone synthesis, thus confirming the conclusion that it arrests cells in G1 slightly before the G1S boundary. However, hydroxyurea did not inhibit the phosphorylation of histone f1 or histone f2a2. The phosphorylation of histone f1, which normally is absent in early G1, begins 2 hr prior to DNA synthesis. In the presence of hydroxyurea, f1 phosphorylation occurs on schedule at this same time in G1, resulting in significant G1-phase f1 phosphorylation. This offers strong evidence that (a) f1 phosphorylation is not restricted to S phase; (b) “old” f1 which was synthesized in previous cell cycles is phosphorylated in G1 before “new” f1 which is synthesized in S phase; and (c) G1-phase f1 phosphorylation does not require new histone or new DNA synthesis. Histone f1 phosphorylation was observed to occur at accelerated rates in S phase over phosphorylation rates observed in late G1-arrest. Data support the proposal that three different levels of f1 phosphorylation occur during the cell cycle: (1) a G1-related phosphorylation of “old” f1; (2) an S-related phosphorylation of both “old” and “new” f1; and (3) a superphosphorylation of f1 associated with chromosome condensation during the G2 to M transition. It is also possible that a limited proportion of f1 may be phosphorylated in G1, perhaps at the initial DNA synthesis sites, and that an increased proportion of f1 is phosphorylated in S as DNA is synthesized. Similarities between the kinetics of histone f1 phosphorylation and the association of DNA with lipoprotein in synchronized control and hydroxyurea-treated cells suggest an involvement of f1 phosphorylation in cell-cycle-dependent chromatin structural changes." @default.
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- W1540521703 date "1974-10-01" @default.
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- W1540521703 title "The metabolism of histone fractions" @default.
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- W1540521703 doi "https://doi.org/10.1016/0003-9861(74)90057-5" @default.
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