甲状腺激素染色质受体活性的调节：类组蛋白样蛋白的可能参与
Regulation of activity of chromatin receptors for thyroid hormone: possible involvement of histone-like proteins.
作者信息
Eberhardt N L, Ring J C, Johnson L K, Latham K R, Apriletti J W, Kitsis R N, Baxter J D
出版信息
Proc Natl Acad Sci U S A. 1979 Oct;76(10):5005-9. doi: 10.1073/pnas.76.10.5005.
Thyroid hormone receptors lose their capability for high-affinity binding of the biologically active triiodothyronine after solubilization and separation from other chromatin proteins. The high-affinity triiodothyronine-binding capacity can be reconstituted by addition of a histone-containing extract of chromatin of purified core histones (H2A, H2B, H3, and H4); a number of other acidic or basic proteins tested were ineffective. The data support a model of the receptor in which a "core" receptor subunit that contains a thyroid hormone-binding site interacts with a regulatory subunit, which is possibly a histone or histone-like species. This interaction with the "core" subunit enables the resulting "holo" receptor to bind biologically active hormones. These data also suggest that histones or related proteins can modulate the activity of nonhistone chromosomal proteins that are involved in regulating the expression of specific genes.
甲状腺激素受体在溶解并与其他染色质蛋白分离后，失去了与生物活性三碘甲状腺原氨酸高亲和力结合的能力。通过添加纯化的核心组蛋白（H2A、H2B、H3和H4）的含组蛋白染色质提取物，可以重建高亲和力三碘甲状腺原氨酸结合能力；测试的许多其他酸性或碱性蛋白均无效。这些数据支持一种受体模型，其中包含甲状腺激素结合位点的“核心”受体亚基与调节亚基相互作用，调节亚基可能是一种组蛋白或类组蛋白。与“核心”亚基的这种相互作用使产生的“全”受体能够结合生物活性激素。这些数据还表明，组蛋白或相关蛋白可以调节参与特定基因表达调控的非组蛋白染色体蛋白的活性。
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