scholarly journals AMF-1/Gps2 Binds p300 and Enhances Its Interaction with Papillomavirus E2 Proteins

2000 ◽  
Vol 74 (13) ◽  
pp. 5872-5879 ◽  
Author(s):  
Yu-Cai Peng ◽  
David E. Breiding ◽  
Francis Sverdrup ◽  
James Richard ◽  
Elliot J. Androphy
Keyword(s):  
Gene Expression ◽  
Transcriptional Activation ◽  
Functional Significance ◽  
Cellular Protein ◽  
Transcriptional Coactivator ◽  
Adenovirus E1a ◽  
Coactivator P300 ◽  
P300 Recruitment

ABSTRACT The cellular protein AMF-1 (Gps2) positively modulates gene expression by the papillomavirus E2 protein (D. E. Breiding et al., Mol. Cell. Biol. 17:7208–7219, 1997). We show here that AMF-1 also binds the transcriptional coactivator p300 in vitro and in vivo. E2 interacted weakly with p300. These observations led to a model in which AMF-1 recruits p300 into a complex with E2. Cotransfection of AMF-1 or p300 stimulated levels of E2-dependent transcription, while cotransfection of both AMF-1 and p300 showed an additive effect. The functional significance of p300 recruitment for E2 transactivation was evidenced by repression of E2-activated transcription by adenovirus E1A, which inhibits both coactivator and acetylase activities of p300. Antibodies to AMF-1 or E2 immunoprecipitated histone acetylase activity from cell lysates. Western blotting using antibody against acetyl-lysine failed to detect acetylation of AMF-1 or E2 in complex with p300. These results suggest that AMF-1 facilitates the recruitment of p300 and its histone acetylase activity into complexes with E2 and represents a novel mechanism of transcriptional activation.

Subnuclear compartmentalization of sequence-specific transcription factors and regulation of eukaryotic gene expression

2005 ◽  
Vol 83 (4) ◽  
pp. 535-547 ◽  
Author(s):  
Gareth N Corry ◽  
D Alan Underhill
Keyword(s):  
Gene Expression ◽  
Transcription Factor ◽  
Transcription Factors ◽  
Transcriptional Activation ◽  
Current Knowledge ◽  
Nuclear Architecture ◽  
Subnuclear Localization ◽  
Modular Structures

To date, the majority of the research regarding eukaryotic transcription factors has focused on characterizing their function primarily through in vitro methods. These studies have revealed that transcription factors are essentially modular structures, containing separate regions that participate in such activities as DNA binding, protein–protein interaction, and transcriptional activation or repression. To fully comprehend the behavior of a given transcription factor, however, these domains must be analyzed in the context of the entire protein, and in certain cases the context of a multiprotein complex. Furthermore, it must be appreciated that transcription factors function in the nucleus, where they must contend with a variety of factors, including the nuclear architecture, chromatin domains, chromosome territories, and cell-cycle-associated processes. Recent examinations of transcription factors in the nucleus have clarified the behavior of these proteins in vivo and have increased our understanding of how gene expression is regulated in eukaryotes. Here, we review the current knowledge regarding sequence-specific transcription factor compartmentalization within the nucleus and discuss its impact on the regulation of such processes as activation or repression of gene expression and interaction with coregulatory factors.Key words: transcription, subnuclear localization, chromatin, gene expression, nuclear architecture.

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.

scholarly journals Yeast Coactivator MBF1 Mediates GCN4-Dependent Transcriptional Activation

1998 ◽  
Vol 18 (9) ◽  
pp. 4971-4976 ◽  
Author(s):  
Ken-ichi Takemaru ◽  
Satoshi Harashima ◽  
Hitoshi Ueda ◽  
Susumu Hirose
Keyword(s):  
Gene Expression ◽  
Saccharomyces Cerevisiae ◽  
Dna Binding ◽  
Nuclear Receptor ◽  
Transcriptional Activation ◽  
Crucial Role ◽  
Tata Binding Protein ◽  
Binding Region

ABSTRACT Transcriptional coactivators play a crucial role in gene expression by communicating between regulatory factors and the basal transcription machinery. The coactivator multiprotein bridging factor 1 (MBF1) was originally identified as a bridging molecule that connects theDrosophila nuclear receptor FTZ-F1 and TATA-binding protein (TBP). The MBF1 sequence is highly conserved across species fromSaccharomyces cerevisiae to human. Here we provide evidence acquired in vitro and in vivo that yeast MBF1 mediates GCN4-dependent transcriptional activation by bridging the DNA-binding region of GCN4 and TBP. These findings indicate that the coactivator MBF1 functions by recruiting TBP to promoters where DNA-binding regulators are bound.

scholarly journals Subregions of the adenovirus E1A transactivation domain target multiple components of the TFIID complex.

1995 ◽  
Vol 15 (11) ◽  
pp. 6283-6290 ◽  
Author(s):  
J V Geisberg ◽  
J L Chen ◽  
R P Ricciardi
Keyword(s):  
Transcriptional Activation ◽  
Terminal Region ◽  
Transactivation Domain ◽  
Adenovirus E1a ◽  
Critical Requirement ◽  
Tata Box Binding Protein ◽  
Carboxy Terminal ◽  
Tfiid Complex

Transcriptional activation by the adenovirus E1A 289R protein requires direct contacts with the TATA box-binding protein (TBP) and also displays a critical requirement for TBP-associated factors (TAFs) (T.G. Boyer and A. J. Berk, Genes Dev. 7:1810-1823, 1993; J. V. Geisberg, W. S. Lee, A. J. Berk, and R. P. Ricciardi, Proc. Natl. Acad. Sci. USA 91:2488-2492, 1994; W. S. Lee, C. C. Kao, G. O. Bryant, X. Liu, and A. J. Berk, Cell 67:365-376, 1991; and Q. Zhou, P. M. Lieberman, T. G. Boyer, and A. J. Berk, Genes Dev. 6:1964-1974, 1992). In this report, we demonstrate that the activation domain of E1A (CR3) specifically binds to two TAFs, human TAFII250 (hTAFII250) and Drosophila TAFII110 (dTAFII110). These interactions can take place both in vivo and in vitro and require the carboxy-terminal region of CR3; the zinc finger region of CR3, which binds TBP, is not needed to bind these TAFs. We mapped the E1A-binding sites on hTAFII250 to an internal region that contains a number of structural motifs, including an HMG box, a bromodomain, and direct repeats. This represents the first demonstration that hTAFII250 may serve as a target of a transcriptional activator. We also mapped the E1A binding on dTAFII110 to its C-terminal region. This is of significance since, by contrast, Sp1-mediated activation requires binding to the N-terminal domain of dTAFII110. Thus, distinct surfaces of dTAFII110 can serve as target sites for different activators. Our results indicate that E1A may activate transcription, in part, through direct contacts of the CR3 subdomains with selected components of the TFIID complex.

scholarly journals A Cellular Repressor of E1A-Stimulated Genes That Inhibits Activation by E2F

1998 ◽  
Vol 18 (9) ◽  
pp. 5032-5041 ◽  
Author(s):  
Elizabeth Veal ◽  
Michael Eisenstein ◽  
Zian H. Tseng ◽  
Grace Gill
Keyword(s):  
Transcriptional Activation ◽  
Transcriptional Control ◽  
Cell Cycle Progression ◽  
Cellular Proliferation ◽  
Sequence Similarity ◽  
Cellular Transformation ◽  
Cellular Protein ◽  
Adenovirus E1a ◽  
E1a Protein

ABSTRACT The adenovirus E1A protein both activates and represses gene expression to promote cellular proliferation and inhibit differentiation. Here we report the identification and characterization of a cellular protein that antagonizes transcriptional activation and cellular transformation by E1A. This protein, termed CREG for cellular repressor of E1A-stimulated genes, shares limited sequence similarity with E1A and binds both the general transcription factor TBP and the tumor suppressor pRb in vitro. In transfection assays, CREG represses transcription and antagonizes 12SE1A-mediated activation of both the adenovirus E2 and cellular hsp70 promoters. CREG also antagonizes E1A-mediated transformation, as expression of CREG reduces the efficiency with which E1A and the oncogeneras cooperate to transform primary cells. Binding sites for E2F, a key transcriptional regulator of cell cycle progression, were found to be required for repression of the adenovirus E2 promoter by CREG, and CREG was shown to inhibit activation by E2F. Since both the adenovirus E1A protein and transcriptional activation by E2F function to promote cellular proliferation, the results presented here suggest that CREG activity may contribute to the transcriptional control of cell growth and differentiation.

scholarly journals Signal-Induced Transcriptional Activation by Dif Requires the dTRAP80 Mediator Module

2003 ◽  
Vol 23 (4) ◽  
pp. 1358-1367 ◽  
Author(s):  
Jin Mo Park ◽  
Jung Mo Kim ◽  
Lark Kyun Kim ◽  
Se Nyun Kim ◽  
Jeongsil Kim-Ha ◽  
...  
Keyword(s):  
Gene Expression ◽  
Transcriptional Activation ◽  
Specific Binding ◽  
Regulation Of Gene Expression ◽  
Transcriptional Activator ◽  
Mediator Complex ◽  
Activator Proteins ◽  
In Vitro Interactions

ABSTRACT The Mediator complex is the major multiprotein transcriptional coactivator complex in Drosophila melanogaster. Mediator components interact with diverse sets of transcriptional activator proteins to elicit the sophisticated regulation of gene expression. The distinct phenotypes associated with certain mutations in some of the Mediator genes and the specific in vitro interactions of Mediator gene products with transcriptional activator proteins suggest the presence of activator-specific binding subunits within the Mediator complex. However, the physiological relevance of these selective in vitro interactions has not been addressed. Therefore, we analyzed dTRAP80, one of the putative activator-binding subunits of the Mediator, for specificity of binding to a number of natural transcriptional activators from Drosophila. Among the group of activator proteins that requires the Mediator complex for transcriptional activation, only a subset of these proteins interacted with dTRAP80 in vitro and only these dTRAP80-interacting activators were defective for activation under dTRAP80-deficient in vivo conditions. In particular, activation of Drosophila antimicrobial peptide drosomycin gene expression by the NF-κB-like transcription factor Dif during induction of the Toll signaling pathway was dependent on the dTRAP80 module. These results, and the indirect support from the dTRAP80 artificial recruitment assay, indicate that dTRAP80 serves as a genuine activator-binding target responsible for a distinct group of activators.

scholarly journals Regulation by glucocorticoids of angiotensinogen gene expression and secretion in adipose cells

1997 ◽  
Vol 328 (2) ◽  
pp. 701-706 ◽  
Author(s):  
Jérôme AUBERT ◽  
Christian DARIMONT ◽  
Irina SAFONOVA ◽  
Gérard AILHAUD ◽  
Raymond NEGREL
Keyword(s):  
Gene Expression ◽  
Adipose Tissue ◽  
Transcriptional Activation ◽  
Ex Vivo ◽  
Activation Product ◽  
Potential Link ◽  
Rat Adipose Tissue ◽  
Adipose Cells

Adipose cells are an important source of angiotensinogen (AT). Its activation product, angiotensin II, stimulates in vitro and in vivo the production and release of prostacyclin which acts as a potent adipogenic signal in promoting the terminal differentiation of preadipocytes to adipocytes. Since glucocorticoids are known to promote adipose cell differentiation in vitro as well as in vivo, their role in the regulation of AT gene expression and secretion has been investigated in cultured Ob1771 mouse adipose cells. In contrast with liver cells, which are the major source of AT and the target of several hormones for the regulation of its expression, adipose cells are only responsive to glucocorticoids, which are able to up-regulate AT gene expression and AT secretion rapidly and dose-dependently. On exposure to glucocorticoids, accumulation of AT mRNA appears primarily to be due to transcriptional activation of the gene and is parallelled by secretion of the protein. Similar results on AT mRNA expression and AT secretion were obtained using explants of rat adipose tissue ex vivo demonstrating a major if not exclusive mechanism of regulation of AT production by glucocorticoids in mature adipose cells. Together these results provide a potential link between glucocorticoids, AT, the growth of adipose tissue and increased blood pressure.

scholarly journals The hsp70 gene CCAAT-binding factor mediates transcriptional activation by the adenovirus E1a protein.

1992 ◽  
Vol 12 (6) ◽  
pp. 2599-2605 ◽  
Author(s):  
L S Lum ◽  
S Hsu ◽  
M Vaewhongs ◽  
B Wu
Keyword(s):  
Transcriptional Activation ◽  
Dependent Manner ◽  
Hsp70 Gene ◽  
Hsp70 Promoter ◽  
Adenovirus E1a ◽  
Cell Biol ◽  
Binding Factor ◽  
E1a Protein

Expression of the human hsp70 gene is cell cycle regulated and is inducible by both serum and the adenovirus E1a protein (K. Milarski and R. Morimoto, Proc. Natl. Acad. Sci. USA 83:9517-9521, 1986; M. C. Simon, K. Kitchener, H.-T. Kao, E. Hickey, L. Weber, R. Voellmy, N. Heintz, and J. R. Nevins, Mol. Cell. Biol. 7:2884-2890, 1987; B. Wu, H. Hurst, N. Jones, and R. Morimoto, Mol. Cell. Biol. 6:2994-2999, 1986; B. Wu and R. Morimoto, Proc. Natl. Acad. Sci. USA 82:6070-6074, 1985). This regulated expression is predominantly controlled by the CCAAT element at position -70 relative to the transcriptional initiation site (G. Williams, T. McClanahan, and R. Morimoto, Mol. Cell. Biol. 9:2574-2587, 1989; B. Wu, H. Hurst, N. Jones, and R. Morimoto, Mol. Cell. Biol. 6:2994-2999, 1986). A corresponding CCAAT-binding factor (CBF) of 999 amino acids has recently been cloned and shown to stimulate transcription selectively from the hsp70 promoter in a CCAAT element-dependent manner (L. Lum, L. Sultzman, R. Kaufman, D. Linzer, and B. Wu, Mol. Cell. Biol. 10:6709-6717, 1990). We report here that the first 192 residues of CBF, when fused to the DNA-binding domain of the heterologous activator GAL-4, are necessary and sufficient to mediate E1a-dependent transcriptional activation. E1a and CBF exhibit complex formation in vitro, suggesting that an in vivo interaction between these proteins may be relevant to the well-characterized E1a-induced transcriptional activation of the hsp70 promoter.

Transcriptional control of plant storage protein genes

1993 ◽  
Vol 342 (1301) ◽  
pp. 209-215 ◽  
Keyword(s):  
Gene Expression ◽  
Transcriptional Activation ◽  
Transcriptional Control ◽  
Storage Proteins ◽  
Promoter Deletion Analysis ◽  
Protein Dna Interactions ◽  
Plant Storage

The accumulation of plant storage proteins is controlled primarily by the transcriptional activation of their genes. Two classes of storage proteins, the zygotic or seed-specific, and the somatic, such as tuber proteins, have been studied. Gene expression analysis in transgenic plants has defined small regions of the promoters of such genes that are able to confer the appropriate patterns of expression. Protein-DNA interactions, both in vivo and in vitro , have revealed proteins that bind to regions implicated in expression, and these may be transcription factors. Promoter deletion analysis has determined the role of some of these DNA-binding proteins, such as in determining tissue-specificity or levels of expression. A common theme linking the expression of both classes of storage proteins is the involvement of metabolite levels in directly controlling gene expression.

scholarly journals Acetylation of β-Catenin by p300 Regulates β-Catenin-Tcf4 Interaction

2004 ◽  
Vol 24 (8) ◽  
pp. 3404-3414 ◽  
Author(s):  
Laurence Lévy ◽  
Yu Wei ◽  
Charlotte Labalette ◽  
Yuanfei Wu ◽  
Claire-Angélique Renard ◽  
...  
Keyword(s):  
Androgen Receptor ◽  
Transcriptional Activity ◽  
Critical Role ◽  
Lysine Acetylation ◽  
Transcriptional Coactivator ◽  
Negative Effects ◽  
Activation Of Transcription ◽  
Coactivator P300

ABSTRACT Lysine acetylation modulates the activities of nonhistone regulatory proteins and plays a critical role in the regulation of cellular gene transcription. In this study, we showed that the transcriptional coactivator p300 acetylated β-catenin at lysine 345, located in arm repeat 6, in vitro and in vivo. Acetylation of this residue increased the affinity of β-catenin for Tcf4, and the cellular Tcf4-bound pool of β-catenin was significantly enriched in acetylated form. We demonstrated that the acetyltransferase activity of p300 was required for efficient activation of transcription mediated by β-catenin/Tcf4 and that the cooperation between p300 and β-catenin was severely reduced by the K345R mutation, implying that acetylation of β-catenin plays a part in the coactivation of β-catenin by p300. Interestingly, acetylation of β-catenin had opposite, negative effects on the binding of β-catenin to the androgen receptor. Our data suggest that acetylation of β-catenin in the arm 6 domain regulates β-catenin transcriptional activity by differentially modulating its affinity for Tcf4 and the androgen receptor. Thus, our results describe a new mechanism by which p300 might regulate β-catenin transcriptional activity.

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