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Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation

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MOLECULAR CELL 2000年第6期5卷 905-915页

作者： Cheung, P Tanner, KG Cheung, WL Sassone-Corsi, P Denu, JM Allis, CD Univ Virginia Dept Biochem & Mol Genet Charlottesville VA 22908 USA Oregon Hlth & Sci Univ Dept Biochem & Mol Biol Portland OR 97201 USA ULP INSERM CNRS Inst Genet & Biol Mol & Cellulaire F-67404 Illkirch Graffenstaden France

Histone acetylation and phosphorylation have separately been suggested to affect chromatin structure and gene expression. Here we report that these two modifications are synergistic. Stimulation of mammalian cells by epidermal growth factor (EGF) results in rapid and sequential phosphorylation and acetylation of H3, and these dimodified H3 molecules are preferentially associated with the EGF-activated c-fos promoter in a MAP kinase-dependent manner. In addition, the prototypical histone acetyltransferase Gcn5 displays an up to 10-fold preference for phosphorylated (Ser-10) H3 over nonphosphorylated H3 as substrate in vitro, suggesting that H3 phosphorylation can affect the efficiency of subsequent acetylation reactions. Together, these results illustrate how the addition of multiple histone modifications may be coupled during the process of gene expression.

关键词：乙酰化作用/药物作用乙酰基转移酶类/化学乙酰基转移酶类/遗传学乙酰基转移酶类/代谢氨基酸序列抗体/免疫学细胞系染色质/遗传学染色质/代谢 DNA结合蛋白质类表皮生长因子/药理学真菌蛋白质类/化学真菌蛋白质类/遗传学真菌蛋白质类/代谢基因表达调控/药物作用基因 fos/遗传学组蛋白酰基转移酶组蛋白类/化学组蛋白类/免疫学组蛋白类/代谢动力学 MAP激酶信号系统/药物作用小鼠近交C3H 丝裂原激活蛋白激酶类/代谢分子序列数据磷酰化/药物作用启动区遗传/遗传学蛋白激酶类/化学蛋白激酶类/遗传学蛋白激酶类/代谢酿酒酵母蛋白质类底物特异性动物小鼠

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In vivo modulation of CYP enzymes by quinidine and rifampin

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CLINICAL PHARMACOLOGY & THERAPEUTICS 2000年第4期68卷 401-411页

作者： Branch, RA Adedoyin, A Frye, RF Wilson, JW Romkes, M Univ Pittsburgh Med Ctr Ctr Clin Pharmacol Pittsburgh PA 15213 USA Univ Pittsburgh Dept Pharmaceut Sci Pittsburgh PA 15213 USA Zeneca Pharmaceut Dept Drug Disposit & Metab Wilmington DE USA

Background: The metabolism of drugs and other xenobiotics is mediated by enzymes whose activities can be modulated by different compounds. The activities of these modulators have the potential to be used to optimize drug action, prevent toxicity, or identify the enzymes involved in a reaction. This approach requires that selective agents be used for specific enzymes. However, selectivity of action has been poorly characterized in vivo. Methods: This study investigated the effect of 3 and 28 days of treatment with quinidine (200 mg daily) and rifampin (INN, rifampicin) (600 mg daily) on the activities of four cytochrome P450 enzymes and N-acetyltransferase in 28 healthy young male volunteers divided into three groups with a cocktail of drug probes used, including caffeine, mephenytoin, debrisoquin (INN, debrisoquine), and dapsone. Results: Quinidine selectively and almost completely inhibited the activity of CYP2D6 from day 3 through day 28 without affecting any other enzymes. Rifampin showed evidence of time-dependent induction of the activities of all measured oxidative routes of metabolism but decreased the acetylation ratio in fast acetylators. The quinidine/rifampin combination resulted in selective CYP2D6 inhibition and induction of all other enzymes evaluated over this time period, suggesting that predictable complex interactions occur with the drug combination. Conclusions: These observations illustrate the value of simultaneous assessment of the effect of modulators on the activities of multiple specific enzymes with the drug cocktail approach.

关键词：乙酰化作用/药物作用投药口服肾上腺素能α拮抗剂/投药和剂量肾上腺素能α拮抗剂/药理学抗心律失常药/药理学抗生素类抗结核/药理学抗惊厥药/药理学芳基烃羟化酶类咖啡因/药理学中枢神经系统刺激剂/药理学细胞色素P450CYP1A2/代谢细胞色素P450CYP2D6/代谢细胞色素P450CYP2E1/代谢细胞色素P450酶系统/拮抗剂和抑制剂细胞色素P450酶系统/代谢氨苯砜/药理学异喹胍/药理学用药计划表酶抑制剂/投药和剂量酶抑制剂/药理学美芬妥英/药理学混合功能氧化酶类/代谢奎尼丁/投药和剂量奎尼丁/药理学参考值利福平/投药和剂量利福平/药理学类固醇16-α-羟化酶甾类羟化酶类/代谢茶碱/药理学成年人人类男(雄)性

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BRG-1 is recruited to estrogen-responsive promoters and cooperates with factors involved in histone acetylation

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MOLECULAR AND CELLULAR BIOLOGY 2000年第20期20卷 7541-7549页

作者： DiRenzo, J Shang, YF Phelan, M Sif, S Myers, M Kingston, R Brown, M D 730 Dana Farber Canc Inst Dept Adult Oncol Boston MA 02115 USA Harvard Univ Sch Med Dept Genet Boston MA 02115 USA Harvard Univ Massachusetts Gen Hosp Sch Med Dept Mol Biol Boston MA 02114 USA

Several factors that mediate activation by nuclear receptors also modify the chemical and structural composition of chromatin. Prominent in this diverse group is the steroid receptor coactivator 1 (SRC-1) family, which interact with agonist-bound nuclear receptors, thereby coupling them to multifunctional transcriptional coregulators such as CREB-binding protein (CBP), p300, and PCAF, all of which have potent histone acetyltransferase activity. Additionally factors including the Brahma-related gene 1 (BRG-1) that are involved in the structural remodeling of chromatin also mediate hormone-dependent transcriptional activation by nuclear receptors. Here, we provide evidence that these two distinct mechanisms of coactivation may operate in a collaborative manner. We demonstrate that transcriptional activation by the estrogen receptor (ER) requires functional BRG-1 and that the coactivation of estrogen signaling by either SRC-1 or CBP is BRG-1 dependent, We find that in response to estrogen, ER recruits BRG-1, thereby targeting BRG-1 to the promoters of estrogen-responsive genes in a manner that occurs simultaneous to histone acetylation. Finally, we demonstrate that BRG-1-mediated coactivation of ER signaling is regulated by the state of histone acetylation within a cell. Inhibition of histone deacetylation by trichostatin A dramatically increases BRG-1-mediated coactivation of ER signaling, and this increase is reversed by overexpression of histone deacetylase 1. These studies support a critical role for BRG-1 in ER action in which estrogen stimulates an ER-BRG-1 association coupling BRG-1 to regions of chromatin at the sites of estrogen-responsive promoters and promotes the activity of other recruited factors that alter the acetylation state of chromatin.

关键词：乙酰化作用/药物作用 CREB结合蛋白质染色质/化学染色质/遗传学染色质/代谢 DNA解旋酶类 DNA结合蛋白质类/代谢雌激素类/药理学组蛋白酰基转移酶组蛋白脱乙酰基酶类/代谢组蛋白类/化学组蛋白类/代谢羟肟酸类/药理学配体核蛋白质类/代谢核受体共激活因子1 启动区遗传/遗传学蛋白质结合/药物作用受体雌激素/代谢反应元件/遗传学信号传导/药物作用反式激活因子类/代谢转录因子/代谢转录激活/药物作用肿瘤细胞培养的人类

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Activation of the BRLF1 promoter and lytic cycle of Epstein-Barr virus by histone acetylation

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NUCLEIC ACIDS RESEARCH 2000年第20期28卷 3918-3925页

作者： Chang, LK Liu, ST Chang Gung Univ Dept Microbiol & Immunol Mol Genet Lab Tao Yuan 333 Taiwan

Histone acetylation alters the chromatin structure and activates the genes that are repressed by histone deacetylation. This investigation demonstrates that treating P3HR1 cells with trichostatin A (TSA) activates the Epstein-Barr virus (EBV) lytic cycle, allowing the virus to synthesize three viral lytic proteins-Rta, Zta and EA-D. Experimental results indicate that TSA and 12-O-tetradecanoylphorbol-13-acetate synergistically activate the transcription of BRLF1, an immediate-early gene of EBV. Chromatin immunoprecipitation assay reveals that histone H4 at the BRLF1 promoter is acetylated after P3HR1 cells are treated with TSA, suggesting that histone acetylation activates BRLF1 transcription. Furthermore, results in this study demonstrate that mutation of a YY1-binding site in the BRLF1 promoter activates BRLF1 transcription 1.6- and 2.3-fold in P3HR1 cells and C33A cells, respectively. Real time PCR analysis reveals that the mutation also increases the histone acetylation level of the nucleosomes at the BRLF1 promoter 1.64- and 3.08-fold in P3HR1 and C33A cells, respectively. Results presented herein suggest that histone deacetylation plays an important role in maintaining the viral latency and histone acetylation at the BRLF1. promoter allows the virus to express Rta and to activate the viral lytic cycle.

关键词：乙酰化作用/药物作用乙酰基转移酶类/拮抗剂和抑制剂乙酰基转移酶类/代谢碱基序列结合部位染色质/化学染色质/药物作用染色质/遗传学染色质/代谢放线菌酮/药理学 DNA结合蛋白质类/生理学药物协同作用红系细胞特异性DNA结合因子类基因表达调控病毒/药物作用基因即早/遗传学基因组病毒疱疹病毒4型人/药物作用疱疹病毒4型人/遗传学疱疹病毒4型人/致病力疱疹病毒4型人/生理学组蛋白酰基转移酶组蛋白类/化学组蛋白类/药物作用组蛋白类/代谢羟肟酸类/药理学即早蛋白质类/遗传学突变沉淀素试验启动区遗传/遗传学 RNA 信使/分析 RNA 信使/生物合成 RNA 信使/遗传学 RNA 病毒/分析 RNA 病毒/生物合成 RNA 病毒/遗传学反应元件/遗传学酿酒酵母蛋白质类十四酰佛波乙酯/药理学反式激活因子类/遗传学转录因子/生理学转录遗传/药物作用转录激活/药物作用转染肿瘤细胞培养的病毒蛋白质类病毒复制/药物作用 YY1转录因子人类

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Hypernuclear acetylation in atherosclerotic lesions and activated vascular smooth muscle cells

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BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 1999年第2期266卷 417-424页

作者： Kawahara, K Watanabe, S Ohshima, T Soejima, Y Oishi, T Aratani, S Nakata, M Shibata, M Inoue, K Amano, T Fujii, R Yanai, K Hagiwara, M Fukamizu, A Maruyama, I Nakajima, T Kagoshima Univ Fac Med Dept Clin Invest Kagoshima 8908520 Japan Med & Biol Labs Co Ltd Dept Tech & Res Nagano 396 Japan Univ Tsukuba Inst Appl Biochem Tsukuba Ibaraki 3058572 Japan Matsue Red Cross Hosp Dept Cardiol Matsue Shimane 667 Japan Tokyo Med & Dent Univ Med Res Inst Dept Funct Genom Tokyo 113 Japan Japan Sci & Technol Corp PRESTO Kyoto Japan

Recent studies have implicated acetylation of several nuclear proteins such as histones and p53 on their epsilon-portion of lysine residues in eukaryotic transcription. Here we raised a specific polyclonal antibody against E-acetylated lysine. Using the antibody, we detected hypernuclear acetylation (HNA) in atherosclerotic vascular smooth muscle cells (VSMCs). Thrombin, a humoral factor known to cause activation and proliferation of VSMCs, strongly potentiated HNA in cultured VSMCs. MAP kinase pathway and a signal coactivator CREB binding protein (CBP) were involved in thrombin-induced HNA of VSMCs. Our results suggest that coactivators cooperating with signal-dependent transcription activators play an important role in atherosclerogenesis via HNA in VSMCs. (C) 1999 Academic Press.

关键词：乙酰化作用/药物作用抗体/免疫学丁二烯类/药理学 CREB结合蛋白质尸体细胞培养的酶激活/药物作用酶抑制剂/药理学血凝素类/代谢免疫组织化学赖氨酸/类似物和衍生物赖氨酸/分析赖氨酸/免疫学丝裂原激活蛋白激酶类/代谢肌平滑血管/代谢腈类/药理学核蛋白质类/化学核蛋白质类/代谢凝血酶/药理学反式激活因子类/代谢转染人类

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