scholarly journals Molecular Basis for the Regulation of Transcriptional Coactivator p300 in Myogenic Differentiation

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Jihong Chen ◽  
Yingjian Wang ◽  
Munerah Hamed ◽  
Natascha Lacroix ◽  
Qiao Li
Keyword(s):  
Molecular Basis ◽  
Myogenic Differentiation ◽  
Transcriptional Coactivator ◽  
Coactivator P300

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 Epstein-Barr Virus Nuclear Antigen 3C and Prothymosin Alpha Interact with the p300 Transcriptional Coactivator at the CH1 and CH3/HAT Domains and Cooperate in Regulation of Transcription and Histone Acetylation

2002 ◽  
Vol 76 (10) ◽  
pp. 4699-4708 ◽  
Author(s):  
Chitra Subramanian ◽  
Sameez Hasan ◽  
Martin Rowe ◽  
Michael Hottiger ◽  
Rama Orre ◽  
...  
Keyword(s):  
Epstein Barr Virus ◽  
Nuclear Antigen ◽  
Regulation Of Transcription ◽  
Transcriptional Coactivator ◽  
Prothymosin Alpha ◽  
Barr Virus ◽  
Amino Terminal ◽  
Epstein Barr ◽  
Coactivator P300

ABSTRACT The Epstein-Barr virus nuclear antigen 3C (EBNA3C), encoded by Epstein-Barr virus (EBV), is essential for mediating transformation of human B lymphocytes. Previous studies demonstrated that EBNA3C interacts with a small, nonhistone, highly acidic, high-mobility group-like nuclear protein prothymosin alpha (ProTα) and the transcriptional coactivator p300 in complexes from EBV-infected cells. These complexes were shown to be associated with histone acetyltransferase (HAT) activity in that they were able to acetylate crude histones in vitro. In this report we show that ProTα interacts with p300 similarly to p53 and other known oncoproteins at the CH1 amino-terminal domain as well as at a second domain downstream of the bromodomain which includes the CH3 region and HAT domain. Similarly, EBNA3C also interacts with p300 at regions which include the CH1 and CH3/HAT domains, suggesting that ProTα and EBNAC3C may interact in a complex with p300. We also show that ProTα activates transcription when targeted to promoters by fusion to the GAL4 DNA binding domain and that this activation is enhanced by the addition of an exogenous source of p300 under the control of a heterologous promoter. This overall activity is down-modulated in the presence of EBNA3C. These results further establish the interaction of cellular coactivator p300 with ProTα and demonstrate that the associated activities resulting from this interaction, which plays a role in acetylation of histones and coactivation, can be regulated by EBNA3C. Furthermore, this study establishes for the first time a transcriptional role for ProTα in recruitment or stabilization of coactivator p300, as well as other basal transcription factors, at the nucleosomes for regulation of transcription.

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