NF-Y is essential for the recruitment of RNA polymerase II and inducible transcription of several CCAAT box-containing genes

NF-Y is essential for the recruitment of RNA polymerase II and inducible transcription of several CCAAT box-containing genes
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DOI:
10.1128/mcb.25.1.512-522.2005
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发表时间:
2005-01-01
影响因子:
5.3
通讯作者:
Handa, H
Handa, H
中科院分区:
生物学2区
文献类型:
--
作者:
Kabe, Y;Yamada, J;Handa, H

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破骨细胞分化因子(ODF)/NF-κB配体受体激活剂对于诱导成熟破骨细胞的分化至关重要。我们发现核因子 Y (NF-Y) 与 ODF 启动子上的 CCAAT 盒结合并调节其基础转录活性。 ODF 基因上的 CCAAT 盒是维生素 D3 转录诱导所必需的,这表明 NF-Y 与 VDR 一起共同调节该启动子。染色质免疫沉淀分析表明,NF-Y 是在 ODF 启动子上招募 RNA 聚合酶 II (RNAPII) 和 TATA 盒结合蛋白所必需的。维生素 D3 刺激促进 VDR 和 p300 募集到 ODF 启动子上,从而以不依赖 NF-Y 的方式导致组蛋白 H4 乙酰化。甲状旁腺激素或前列腺素 E 诱导 ODF 基因也依赖于 NF-Y。此外,NF-Y 对于将 RNAPII 招募到其他含有 CCAAT 盒的启动子(例如骨桥蛋白、CYP24 和 E2F1 的启动子)上至关重要。这些结果表明,NF-Y 响应各种诱导,将 RNAPII 和一般转录因子募集到各种含有 CCAAT 盒的启动子上,以允许独立于组蛋白修饰的强转录激活。
Osteoclast differentiation factor (ODF)/receptor activator of NF-kappaB ligand is essential for inducing the differentiation of mature osteoclasts. We find that nuclear factor Y (NF-Y) binds to the CCAAT box on the ODF promoter and regulates its basal transcriptional activity. The CCAAT box on the ODF gene is required for its transcriptional induction by vitamin D3, suggesting that NF-Y coregulates this promoter along with VDR. Chromatin immunoprecipitation analysis reveals that NF-Y is required for the recruitment of RNA polymerase II (RNAPII) and TATA box binding protein on the ODF promoter. Stimulation with vitamin D3 facilitates the recruitment of VDR and p300 onto the ODF promoter, resulting in acetylation of histone H4 in an NF-Y-independent manner. ODF gene induction by parathyroid hormone or prostaglandin E is also dependent on NF-Y. Furthermore, NF-Y is essential for the recruitment of RNAPII onto other CCAAT box-containing promoters, such as those of osteopontin, CYP24, and E2F1. These results suggest that NF-Y recruits RNAPII and general transcription factors onto various CCAAT box-containing promoters in response to various inductions to permit strong transcriptional activation independently of histone modifications.