共查询到20条相似文献,搜索用时 15 毫秒
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Eliot L. Osher Francisco Castillo Nagarajan Elumalai Michael J. Waring Garry Pairaudeau Ali Tavassoli 《Bioorganic & medicinal chemistry》2018,26(11):3034-3038
We report an inhibitor of the homodimeric protein-protein interaction of the BCL6 oncoprotein, identified from a genetically encoded SICLOPPS library of 3.2 million cyclic hexapeptides in combination with a bacterial reverse two-hybrid system. This cyclic peptide is shown to bind the BTB domain of BCL6, disrupts its homodimerization, and subsequent binding of the SMRT2 corepressor peptide. 相似文献
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The ETO protein disrupted in t(8;21)-associated acute myeloid leukemia is a corepressor for the promyelocytic leukemia zinc finger protein 总被引:11,自引:0,他引:11
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Melnick AM Westendorf JJ Polinger A Carlile GW Arai S Ball HJ Lutterbach B Hiebert SW Licht JD 《Molecular and cellular biology》2000,20(6):2075-2086
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Andrew C. Pearce Mark J. Bamford Ruth Barber Angela Bridges Maire A. Convery Constantinos Demetriou Sian Evans Thomas Gobbetti David J. Hirst Duncan S. Holmes Jonathan P. Hutchinson Sandrine Jayne Larissa Lezina Michael T. McCabe Cassie Messenger Joanne Morley Melissa C. Musso Paul Scott-Stevens Ana Sousa Manso Jennifer Schofield Tom Slocombe Don Somers Ann L. Walker Anastasia Wyce Xi-Ping Zhang Simon D. Wagner 《The Journal of biological chemistry》2021,297(2)
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A SANT motif in the SMRT corepressor interprets the histone code and promotes histone deacetylation 总被引:7,自引:0,他引:7
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Nuclear receptor corepressors SMRT (silencing mediator of retinoid and thyroid receptors) and N-CoR (nuclear receptor corepressor) recruit histone deacetylase (HDAC) activity to targeted regions of chromatin. These corepressors contain a closely spaced pair of SANT motifs whose sequence and organization is highly conserved. The N-terminal SANT is a critical component of a deacetylase activation domain (DAD) that binds and activates HDAC3. Here, we show that the second SANT motif functions as part of a histone interaction domain (HID). The HID enhances repression by increasing the affinity of the DAD-HDAC3 enzyme for histone substrate. The two SANT motifs synergistically promote histone deacetylation and repression through unique functions. The HID contribution to repression is magnified by its ability to inhibit histone acetyltransferase enzyme activity. Remarkably, the SANT-containing HID preferentially binds to unacetylated histone tails. This implies that the SMRT HID participates in interpreting the histone code in a feed-forward mechanism that promotes and maintains histone deacetylation at genomic sites of SMRT recruitment. 相似文献
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Webb P Valentine C Nguyen P Price RH Marimuthu A West BL Baxter JD Kushner PJ 《Nuclear receptor》2003,1(1):4
Nuclear receptors (NRs) usually bind the corepressors N-CoR and SMRT in the absence of ligand or in the presence of antagonists. Agonist binding leads to corepressor release and recruitment of coactivators. Here, we report that estrogen receptor beta (ERbeta) binds N-CoR and SMRT in the presence of agonists, but not antagonists, in vitro and in vivo. This ligand preference differs from that of ERalpha interactions with corepressors, which are inhibited by estradiol, and resembles that of ERbeta interactions with coactivators. ERbeta /N-CoR interactions involve ERbeta AF-2, which also mediates coactivator recognition. Moreover, ERbeta recognizes a sequence (PLTIRML) in the N-CoR C-terminus that resembles coactivator LXXLL motifs. Inhibition of histone deacetylase activity specifically potentiates ERbeta LBD activity, suggesting that corepressors restrict the activity of AF-2. We conclude that the ER isoforms show completely distinct modes of interaction with a physiologically important corepressor and discuss our results in terms of ER isoform specificity in vivo. 相似文献
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