scholarly journals Transcriptional Coactivator p300/CBP-Associated Factor and p300/CBP-Associated Factor Type B Are Required for Normal Estrogen Response of the Mouse Uterus

2004 ◽  
Vol 68 (10) ◽  
pp. 2209-2211 ◽  
Author(s):  
Erina INOUE ◽  
Miho HANAI ◽  
Kazuhiko YAMADA ◽  
Takatoshi ESASHI ◽  
Jun YAMAUCHI
Keyword(s):  
Transcriptional Coactivator ◽  
Type B ◽  
Mouse Uterus ◽  
Associated Factor ◽  
Estrogen Response ◽  
Factor Type ◽  
Coactivator P300

Regulation of HOXA10 expression by phytoestrogens

2007 ◽  
Vol 292 (2) ◽  
pp. E435-E442 ◽  
Author(s):  
G. Eda Akbas ◽  
Xiaolan Fei ◽  
Hugh S. Taylor
Keyword(s):  
Estrogen Receptor ◽  
Estrogen Receptor Α ◽  
In Utero ◽  
Estrogen Response Element ◽  
Mouse Uterus ◽  
Response Element ◽  
Estrogen Response ◽  
Uterine Anomalies ◽  
Mrna And Protein Expression ◽  
Adult Exposure

HOXA10 is necessary for normal development of the Müllerian duct, and continued adult expression in the uterus is necessary for female fertility. HOXA10 expression is altered by diethylstilbestrol, leading to uterine anomalies. Other endocrine disruptors may potentially lead to reproductive anomalies or dysfunction by altering HOXA10 expression. Here we investigated the effect of isoflavones on HOXA10 expression after in utero or adult exposure in the mouse. Genistein, but not diadzein, regulated HOXA10 mRNA and protein expression in the adult mouse uterus. In contrast, in utero genistein or diadzein exposure had no lasting effect on HOXA10 expression in the exposed offspring. Reporter gene expression driven by the HOXA10 estrogen response element was increased in a dose-responsive manner by genistein, but not daidzein. Neither estrogen receptor-α nor estrogen receptor-β binding to the HOXA10 estrogen response element was affected by genistein or daidzein. In utero exposure to isoflavones is unlikely to result in HOXA10-mediated developmental anomalies. Adult genistein exposure alters uterine HOXA10 expression, a potential mechanism by which this agent affects fertility.

scholarly journals Adenovirus E1A specifically blocks SWI/SNF-dependent transcriptional activation.

1996 ◽  
Vol 16 (10) ◽  
pp. 5737-5743 ◽  
Author(s):  
M E Miller ◽  
B R Cairns ◽  
R S Levinson ◽  
K R Yamamoto ◽  
D A Engel ◽  
...  
Keyword(s):  
Transcriptional Activation ◽  
Cellular Transformation ◽  
Transcriptional Coactivator ◽  
Gene Encoding ◽  
Adenovirus E1a ◽  
Transcriptional Regulatory ◽  
Genes Encoding ◽  
Regulatory Complex ◽  
Activation Pathways ◽  
Coactivator P300

Expression of the adenovirus E1A243 oncoprotein in Saccharomyces cerevisiae produces a slow-growth phenotype with accumulation of cells in the G1 phase of the cell cycle. This effect is due to the N-terminal and CR1 domains of E1A243, which in rodent cells are involved in triggering cellular transformation and also in binding to the cellular transcriptional coactivator p300. A genetic screen was undertaken to identify genes required for the function of E1A243 in S. cerevisiae. This screen identified SNF12, a gene encoding the 73-kDa subunit of the SWI/SNF transcriptional regulatory complex. Mutation of genes encoding known members of the SWI/SNF complex also led to loss of E1A function, suggesting that the SWI/SNF complex is a target of E1A243. Moreover, expression of E1A in wild-type cells specifically blocked transcriptional activation of the INO1 and SUC2 genes, whose activation pathways are distinct but have a common requirement for the SWI/SNF complex. These data demonstrate a specific functional interaction between E1A and the SWI/SNF complex and suggest that a similar interaction takes place in rodent and human cells.

Natural derivatives of curcumin attenuate the Wnt/β-catenin pathway through down-regulation of the transcriptional coactivator p300

2008 ◽  
Vol 377 (4) ◽  
pp. 1304-1308 ◽  
Author(s):  
Min-Jung Ryu ◽  
Munju Cho ◽  
Jie-Young Song ◽  
Yeon-Sook Yun ◽  
Il-Whan Choi ◽  
...  
Keyword(s):  
Transcriptional Coactivator ◽  
Down Regulation ◽  
Derivatives Of ◽  
Coactivator P300

scholarly journals Scaffold/Matrix Attachment Region Elements Interact with a p300-Scaffold Attachment Factor A Complex and Are Bound by Acetylated Nucleosomes

2002 ◽  
Vol 22 (8) ◽  
pp. 2598-2606 ◽  
Author(s):  
Joost H. A. Martens ◽  
Matty Verlaan ◽  
Eric Kalkhoven ◽  
Josephine C. Dorsman ◽  
Alt Zantema
Keyword(s):  
Nuclear Matrix ◽  
Topoisomerase I ◽  
Matrix Attachment Region ◽  
Major Constituent ◽  
Regulation Of Transcription ◽  
Transcriptional Coactivator ◽  
Attachment Region ◽  
Attachment Factor ◽  
Coactivator P300 ◽  
I Gene

ABSTRACT The transcriptional coactivator p300 regulates transcription by binding to proteins involved in transcription and by acetylating histones and other proteins. These transcriptional effects are mainly at promoter and enhancer elements. Regulation of transcription also occurs through scaffold/matrix attachment regions (S/MARs), the chromatin regions that bind the nuclear matrix. Here we show that p300 binds to the S/MAR binding protein scaffold attachment factor A (SAF-A), a major constituent of the nuclear matrix. Using chromatin immunoprecipitations, we established that both p300 and SAF-A bind to S/MAR elements in the transiently silent topoisomerase I gene prior to its activation at G1 during cell cycle. This binding is accompanied by local acetylation of nucleosomes, suggesting that p300-SAF-A interactions at S/MAR elements of nontranscribed genes might poise these genes for transcription.

scholarly journals β-Catenin (CTNNB1) in the Mouse Uterus During Decidualization and the Potential Role of Two Pathways in Regulating Its Degradation

2007 ◽  
Vol 55 (9) ◽  
pp. 963-974 ◽  
Author(s):  
Jennifer L. Herington ◽  
JiaJia Bi ◽  
John D. Martin ◽  
Brent M. Bany
Keyword(s):  
Binding Protein ◽  
E3 Ligase ◽  
Progressive Increase ◽  
Pregnant Mouse ◽  
Transcriptional Coactivator ◽  
Mouse Uterus ◽  
Endometrial Stromal Cells ◽  
Pregnant Uterus ◽  
Steady State Levels

β-catenin plays a role in cell adhesion and as a transcriptional coactivator. Its levels are regulated in cells by controlling its degradation through ubiquitination by two different E3 ligase complexes. One complex contains β-transducing repeat containing (BTRC) protein, which binds to β-catenin when phosphorylated on specific (S33 and S37) residues, whereas the other involves calcyclin-binding protein (CACYBP). The aim of this study was to determine the localization and levels of total and active (S33/S37-dephosphorylated) β-catenin in the pregnant mouse uteri and those undergoing artificially stimulated decidualization. These two forms of β-catenin were localized almost exclusively to the endometrial epithelia just prior to the onset of implantation. Although this localization continued after the onset of implantation, there were less epithelial cells present in areas of the uterus undergoing decidualization. Rather, there was a progressive increase in β-catenin localization in endometrial stromal cells undergoing decidualization in the anti-mesometrial and, to a lesser extent, in the mesometrial regions. The presence of a conceptus was not required for the changes in localization seen in the pregnant uterus because similar findings were also seen in uteri undergoing artificially stimulated decidualization. Finally, overall levels of total, active (S33 and S37 dephosphorylated), and phosphorylated (S33/S37/T42) β-catenin protein and the steady-state levels of calcyclin-binding protein mRNA changed in the uterus during decidualization. The result of this study shows the changing localization and levels of β-catenin in the mouse uterus during decidualization. Further, the results suggest potential roles for both the BTRC and CACYBP E3 ligase mechanisms of β-catenin ubiquitination in the uterus during decidualization.

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