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与早熟染色体凝集维持相关的组蛋白H3磷酸化的特定位点。催化诱导的亚基互换的证据。

Specific site of histone H3 phosphorylation related to the maintenance of premature chromosome condensation. Evidence for catalytically induced interchange of the subunits.

作者信息

Ajiro K, Nishimoto T

出版信息

J Biol Chem. 1985 Dec 15;260(29):15379-81.

PMID:4066674
Abstract

Previously we have found that histone H1 and H3 of tsBN2 cells showing premature chromosome condensation (PCC) at nonpermissive temperature (40.5 degrees C) were phosphorylated extensively as in mitotic cells (Ajiro, K., Nishimoto, T., and Takahashi, T. (1983) J. Biol. Chem. 258, 4534-4538). Under the influence of various chemicals, both the prevention of the PCC induction and the suppression of H3 phosphorylation occurred simultaneously, whereas H1 phosphorylation did not. At the minimum concentration for the inhibition of PCC induction, H1 phosphorylation remained at the control level, but H3 phosphorylation was completely suppressed. Tryptic peptide analysis revealed that the H3 phosphopeptide in PCC was single, and it was observed in the same position as in mitosis. The results suggest that specific site(s) of H3 phosphorylation related to the maintenance of a condensed state of chromatin.

摘要

此前我们发现，tsBN2细胞的组蛋白H1和H3在非允许温度（40.5摄氏度）下呈现早熟染色体凝集（PCC），其磷酸化程度与有丝分裂细胞中的情况一样广泛（秋乃，K.，西本，T.，以及高桥，T.（1983年）《生物化学杂志》258卷，4534 - 4538页）。在各种化学物质的影响下，PCC诱导的预防和H3磷酸化的抑制同时发生，而H1磷酸化则不然。在抑制PCC诱导的最低浓度下，H1磷酸化保持在对照水平，但H3磷酸化被完全抑制。胰蛋白酶肽分析表明，PCC中的H3磷酸肽是单一的，并且在与有丝分裂相同的位置被观察到。结果表明，H3磷酸化的特定位点与染色质凝聚状态的维持有关。

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J Biol Chem. 1985 Dec 15;260(29):15379-81.
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