scholarly journals The Developmental Regulator Protein Gon4l Associates with Protein YY1, Co-repressor Sin3a, and Histone Deacetylase 1 and Mediates Transcriptional Repression

2011 ◽  
Vol 286 (20) ◽  
pp. 18311-18319 ◽  
Author(s):  
Ping Lu ◽  
Isaiah L. Hankel ◽  
Bruce S. Hostager ◽  
Julie A. Swartzendruber ◽  
Ann D. Friedman ◽  
...  
Keyword(s):  
Histone Deacetylase ◽  
Transcriptional Repression ◽  
Histone Deacetylase 1 ◽  
Regulator Protein

scholarly journals Transcriptional repression ofAurora-Agene by wild-type p53 through directly binding to its promoter with histone deacetylase 1 and mSin3a

2017 ◽  
Vol 142 (1) ◽  
pp. 92-108
Author(s):  
Tsung-Ying Yang ◽  
Chieh-Lin Jerry Teng ◽  
Tsung-Chieh Chester Lin ◽  
Kun-Chieh Chen ◽  
Shih-Lan Hsu ◽  
...  
Keyword(s):  
Histone Deacetylase ◽  
Transcriptional Repression ◽  
Wild Type ◽  
Histone Deacetylase 1 ◽  
Wild Type P53

scholarly journals Transcriptional Repression by the SMRT-mSin3 Corepressor: Multiple Interactions, Multiple Mechanisms, and a Potential Role for TFIIB

1998 ◽  
Vol 18 (9) ◽  
pp. 5500-5510 ◽  
Author(s):  
Chi-Wai Wong ◽  
Martin L. Privalsky
Keyword(s):  
Histone Deacetylase ◽  
Transcriptional Repression ◽  
Hormone Receptors ◽  
Alternative Pathway ◽  
Eukaryotic Transcription ◽  
Histone Deacetylase 1 ◽  
General Transcription Factor ◽  
Corepressor Complex ◽  
Chromatin Template ◽  
Physical Interactions

ABSTRACT A variety of eukaryotic transcription factors, including the nuclear hormone receptors, Max-Mad, BCL-6, and PLZF, appear to mediate transcriptional repression through the ability to recruit a multiprotein corepressor complex to the target promoter. This corepressor complex includes the SMRT/N-CoR polypeptides, mSin3A or -B, and histone deacetylase 1 or 2. The presence of a histone-modifying activity in the corepressor complex has led to the suggestion that gene silencing is mediated by modification of the chromatin template, perhaps rendering it less accessible to the transcriptional machinery. We report here, however, that the corepressor complex actually appears to exhibit multiple mechanisms of transcriptional repression, only one of which corresponds with detectable recruitment of the histone deacetylase. We provide evidence instead of an alternative pathway of repression that may be mediated by direct physical interactions between components of the corepressor complex and the general transcription factor TFIIB.

scholarly journals Histone Deacetylase 1 Can Repress Transcription by Binding to Sp1

1999 ◽  
Vol 19 (8) ◽  
pp. 5504-5511 ◽  
Author(s):  
Angelika Doetzlhofer ◽  
Hans Rotheneder ◽  
Gerda Lagger ◽  
Manfred Koranda ◽  
Vladislav Kurtev ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Histone Deacetylase ◽  
Transcriptional Repression ◽  
Trichostatin A ◽  
Dependent Manner ◽  
Histone Deacetylase 1 ◽  
3T3 Fibroblasts ◽  
C Terminus ◽  
Histone Deacetylase Inhibitor Trichostatin ◽  
Carboxy Terminal

ABSTRACT The members of the Sp1 transcription factor family can act as both negative and positive regulators of gene expression. Here we show that Sp1 can be a target for histone deacetylase 1 (HDAC1)-mediated transcriptional repression. The histone deacetylase inhibitor trichostatin A activates the chromosomally integrated murine thymidine kinase promoter in an Sp1-dependent manner. Coimmunoprecipitation experiments with Swiss 3T3 fibroblasts and 293 cells demonstrate that Sp1 and HDAC1 can be part of the same complex. The interaction between Sp1 and HDAC1 is direct and requires the carboxy-terminal domain of Sp1. Previously we have shown that the C terminus of Sp1 is necessary for the interaction with the transcription factor E2F1 (J. Karlseder, H. Rotheneder, and E. Wintersberger, Mol. Cell. Biol. 16:1659–1667, 1996). Coexpression of E2F1 interferes with HDAC1 binding to Sp1 and abolishes Sp1-mediated transcriptional repression. Our results indicate that one component of Sp1-dependent gene regulation involves competition between the transcriptional repressor HDAC1 and the transactivating factor E2F1.

scholarly journals Retinoblastoma Protein Transcriptional Repression through Histone Deacetylation of a Single Nucleosome

2002 ◽  
Vol 22 (3) ◽  
pp. 856-865 ◽  
Author(s):  
Ashby J. Morrison ◽  
Claude Sardet ◽  
Rafael E. Herrera
Keyword(s):  
Histone Deacetylase ◽  
Transcriptional Repression ◽  
Cell Cycle Progression ◽  
Cyclin E ◽  
Retinoblastoma Protein ◽  
Histone Deacetylation ◽  
Cycle Progression ◽  
Histone Deacetylase 1 ◽  
Thiol Reactivity

ABSTRACT The retinoblastoma protein, pRb, controls transcription through recruitment of histone deacetylase to particular E2F-responsive genes. We determined the acetylation level of individual nucleosomes present in the cyclin E promoter of RB +/+ and RB −/− mouse embryo fibroblasts. We also determined the effects of pRb on nucleosomal conformation by examining the thiol reactivity of histone H3 of individual nucleosomes. We found that pRb represses the cyclin E promoter through histone deacetylation of a single nucleosome, to which it and histone deacetylase 1 bind. In addition, the conformation of this nucleosome is modulated by pRb-directed histone deacetylase activity. Thus, the repressive role of pRb in cyclin E transcription and therefore cell cycle progression can be mapped to its control of the acetylation status and conformation of a single nucleosome.

scholarly journals Corepressor MMTR/DMAP1 Is Involved in both Histone Deacetylase 1- and TFIIH-Mediated Transcriptional Repression

2007 ◽  
Vol 27 (10) ◽  
pp. 3578-3588 ◽  
Author(s):  
Bong Gu Kang ◽  
June Ho Shin ◽  
Jae Kyu Yi ◽  
Ho Chul Kang ◽  
Jong Joo Lee ◽  
...  
Keyword(s):  
Histone Deacetylase ◽  
Transcriptional Repression ◽  
Trichostatin A ◽  
Embryonic Stem ◽  
Mouse Embryonic Stem Cell ◽  
Dominant Negative ◽  
Luciferase Reporter ◽  
Histone Deacetylase 1 ◽  
Wide Range

ABSTRACT A transcription corepressor, MAT1-mediated transcriptional repressor (MMTR), was found in mouse embryonic stem cell lines. MMTR orthologs (DMAP1) are found in a wide variety of life forms from yeasts to humans. MMTR down-regulation in differentiating mouse embryonic stem cells in vitro resulted in activation of many unrelated genes, suggesting its role as a general transcriptional repressor. In luciferase reporter assays, the transcriptional repression activity resided at amino acids 221 to 468. Histone deacetylase 1 (HDAC1) interacts with MMTR both in vitro and in vivo and also interacts with MMTR in the nucleus. Interestingly, MMTR activity was only partially rescued by competition with dominant-negative HDAC1(H141A) or by treatment with an HDAC inhibitor, trichostatin A (TSA). To identify the protein responsible for HDAC1-independent MMTR activity, we performed a yeast two-hybrid screen with the full-length MMTR coding sequence as bait and found MAT1. MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase which constitutes a subcomplex of TFIIH. The coiled-coil domain in the middle of MAT1 was confirmed to interact with the C-terminal half of MMTR, and the MMTR-mediated transcriptional repression activity was completely restored by MAT1 in the presence of TSA. Moreover, intact MMTR was required to inhibit phosphorylation of the C-terminal domain in the RNA polymerase II largest subunit by TFIIH kinase in vitro. Taken together, these data strongly suggest that MMTR is part of the basic cellular machinery for a wide range of transcriptional regulation via interaction with TFIIH and HDAC.

scholarly journals The Bovine Herpesvirus 1 Immediate-Early Protein (bICP0) Associates with Histone Deacetylase 1 To Activate Transcription

2001 ◽  
Vol 75 (20) ◽  
pp. 9571-9578 ◽  
Author(s):  
Yange Zhang ◽  
Clinton Jones
Keyword(s):  
Histone Deacetylase ◽  
Transcriptional Repression ◽  
Ring Finger ◽  
Bovine Herpesvirus ◽  
Productive Infection ◽  
Cell Protein ◽  
Bovine Herpesvirus 1 ◽  
Histone Deacetylase 1 ◽  
Early Protein ◽  
Herpesvirus 1

ABSTRACT Infected-cell protein 0 encoded by bovine herpesvirus 1 (BHV-1) (bICP0) is necessary for efficient productive infection, in large part, because it activates all 3 classes of BHV-1 genes (U. V. Wirth, C. Fraefel, B. Vogt, C. Vlcek, V. Paces, and M. Schwyzer, J. Virol. 66:2763–2772, 1992). Although bICP0 is believed to be a functional homologue of herpes simplex virus type 1-encoded ICP0, the only well-conserved domain between the proteins is a zinc ring finger located near the amino terminus of both proteins. Our previous studies demonstrated that bICP0 is toxic to transfected cells but does not appear to directly induce apoptosis (Inman, M., Y. Zhang, V. Geiser, and C. Jones, J. Gen. Virol. 82:483–492, 2001). C-terminal sequences in the last 320 amino acids of bICP0 mediate subcellular localization. Mutagenesis of the zinc ring finger within bICP0 revealed that this domain was important for transcriptional activation. In this study, we demonstrate that bICP0 interacts with histone deacetylase 1 (HDAC1), which results in activation of a simple promoter containing four consensus Myc-Max binding sites. The interaction between bICP0 and HDAC1 correlated with inhibition of Mad-dependent transcriptional repression. In resting CV-1 cells, bICP0 relieved HDAC1-mediated transcriptional repression. The zinc ring finger was required for relieving HDAC1-induced repression but not for interacting with HDAC1. In fetal bovine lung cells but not in a human epithelial cell line, bICP0 expression correlated with reduced steady-state levels of HDAC1 in crude cytoplasmic extracts. We hypothesize that the ability of bICP0 to overcome HDAC1-induced repression plays a role in promoting productive infection in highly differentiated cell types.

scholarly journals 8a, a New Acridine Antiproliferative and Pro-Apoptotic Agent Targeting HDAC1/DNMT1

2021 ◽  
Vol 22 (11) ◽  
pp. 5516
Author(s):  
Qiting Zhang ◽  
Ziyan Wang ◽  
Xinyuan Chen ◽  
Haoxiang Qiu ◽  
Yifan Gu ◽  
...  
Keyword(s):  
Histone Deacetylase ◽  
Dna Methyltransferase ◽  
Hdac Inhibitors ◽  
Mitochondrial Pathway ◽  
Epigenetic Therapy ◽  
Protein Interaction Data ◽  
Dependent Manner ◽  
Histone Deacetylase 1 ◽  
Histiocytic Lymphoma ◽  
Dose Dependent

Epigenetic therapy using histone deacetylase (HDAC) inhibitors has become an attractive project in new drug development. However, DNA methylation and histone acetylation are important epigenetic ways to regulate the occurrence and development of leukemia. Given previous studies, N-(2-aminophenyl)benzamide acridine (8a), as a histone deacetylase 1 (HDAC1) inhibitor, induces apoptosis and shows significant anti-proliferative activity against histiocytic lymphoma U937 cells. HDAC1 plays a role in the nucleus, which we confirmed by finding that 8a entered the nucleus. Subsequently, we verified that 8a mainly passes through the endogenous (mitochondrial) pathway to induce cell apoptosis. From the protein interaction data, we found that 8a also affected the expression of DNA methyltransferase 1 (DNMT1). Therefore, an experiment was performed to assess the binding of 8a to DNMT1 at the molecular and cellular levels. We found that the binding strength of 8a to DNMT1 enhanced in a dose-dependent manner. Additionally, 8a inhibits the expression of DNMT1 mRNA and its protein. These findings suggested that the anti-proliferative and pro-apoptotic activities of 8a against leukemia cells were achieved by targeting HDAC1 and DNMT1.

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