scholarly journals Transcription enhancer factor 1 interacts with a basic helix-loop-helix zipper protein, Max, for positive regulation of cardiac alpha-myosin heavy-chain gene expression.

1997 ◽  
Vol 17 (7) ◽  
pp. 3924-3936 ◽  
Author(s):  
M P Gupta ◽  
C S Amin ◽  
M Gupta ◽  
N Hay ◽  
R Zak
Keyword(s):  
Myosin Heavy Chain ◽  
Reporter Gene ◽  
Heavy Chain ◽  
Troponin T ◽  
Basic Helix Loop Helix ◽  
Helix Loop Helix ◽  
E Box ◽  
Two Factors ◽  
Transcription Enhancer ◽  
Enhancer Factor

The M-CAT binding factor transcription enhancer factor 1 (TEF-1) has been implicated in the regulation of several cardiac and skeletal muscle genes. Previously, we identified an E-box-M-CAT hybrid (EM) motif that is responsible for the basal and cyclic AMP-inducible expression of the rat cardiac alpha-myosin heavy chain (alpha-MHC) gene in cardiac myocytes. In this study, we report that two factors, TEF-1 and a basic helix-loop-helix leucine zipper protein, Max, bind to the alpha-MHC EM motif. We also found that Max was a part of the cardiac troponin T M-CAT-TEF-1 complex even when the DNA template did not contain an apparent E-box binding site. In the protein-protein interaction assay, a stable association of Max with TEF-1 was observed when glutathione S-transferase (GST)-TEF-1 or GST-Max was used to pull down in vitro-translated Max or TEF-1, respectively. In addition, Max was coimmunoprecipitated with TEF-1, thus documenting an in vivo TEF-1-Max interaction. In the transient transcription assay, overexpression of either Max or TEF-1 resulted a mild activation of the alpha-MHC-chloramphenicol acetyltransferase (CAT) reporter gene at lower concentrations and repression of this gene at higher concentrations. However, when Max and TEF-1 expression plasmids were transfected together, the repression mediated by a single expression plasmid was alleviated and a three- to fourfold transactivation of the alpha-MHC-CAT reporter gene was observed. This effect was abolished once the EM motif in the promoter-reporter construct was mutated, thus suggesting that the synergistic transactivation function of the TEF-1-Max heterotypic complex is mediated through binding of the complex to the EM motif. These results demonstrate a novel association between Max and TEF-1 and indicate a positive cooperation between these two factors in alpha-MHC gene regulation.

Expression of raf oncogenes activates the PEA1 transcription factor motif

1989 ◽  
Vol 9 (5) ◽  
pp. 2247-2250
Author(s):  
C Wasylyk ◽  
B Wasylyk ◽  
G Heidecker ◽  
M Huleihel ◽  
U R Rapp
Keyword(s):  
Transcription Factor ◽  
Binding Site ◽  
Atp Binding ◽  
Enhancer Activity ◽  
Atp Binding Site ◽  
Transcription Factor Motif ◽  
Transcription Enhancer

PEA1 (AP1) motif transcription enhancer activity was stimulated by v-raf and more efficiently by activated c-raf-1 or A-raf than by their normal counterparts, in agreement with a role for PEA1 in transformation by raf. Mutations in the ATP-binding site of v-raf prevented activation, suggesting that phosphorylation is somehow required.

scholarly journals The Roles of the Histone Protein Modifier EZH2 in the Uterus and Placenta

Epigenomes ◽  
2020 ◽  
Vol 4 (3) ◽  
pp. 20
Author(s):  
Ana M. Mesa ◽  
Cheryl S. Rosenfeld ◽  
Geetu Tuteja ◽  
Theresa I. Medrano ◽  
Paul S. Cooke
Keyword(s):  
Critical Role ◽  
Histone H3 ◽  
Gene Promoter ◽  
Epigenetic Changes ◽  
Promoter Regions ◽  
Polycomb Repressive Complex 2 ◽  
Gene Sets ◽  
Ezh2 Expression ◽  
And Function ◽  
Transcription Enhancer

Epigenetic modifications regulate normal physiological, as well as pathological processes in various organs, including the uterus and placenta. Both organs undergo dramatic and rapid restructuring that depends upon precise orchestration of events. Epigenetic changes that alter transcription and translation of gene-sets regulate such responses. Histone modifications alter the chromatin structure, thereby affecting transcription factor access to gene promoter regions. Binding of histones to DNA is regulated by addition or removal of subunit methyl and other groups, which can inhibit or stimulate transcription. Enhancer of zeste homolog 2 (EZH2) is the catalytic subunit of polycomb repressive complex 2 (PRC2) that catalyzes tri-methylation of histone H3 at Lys 27 (H3K27me3) and subsequently suppresses transcription of genes bound by such histones. Uterine EZH2 expression exerts a critical role in development and function of this organ with deletion of this gene resulting in uterine hyperplasia and expression of cancer-associated transcripts. Elucidating the roles of EZH2 in uterus and placenta is essential as EZH2 dysregulation is associated with several uterine and placental pathologies. Herein, we discuss EZH2 functions in uterus and placenta, emphasizing its physiological and pathological importance.

scholarly journals A transcription enhancer in the Herpesvirus saimiri genome.

1985 ◽  
Vol 4 (10) ◽  
pp. 2669-2674 ◽  
Author(s):  
S. Schirm ◽  
F. Weber ◽  
W. Schaffner ◽  
B. Fleckenstein
Keyword(s):  
Herpesvirus Saimiri ◽  
Transcription Enhancer

scholarly journals Striking homology between mouse and human transcription enhancer factor-1 (TEF-1)

1993 ◽  
Vol 21 (3) ◽  
pp. 747-748 ◽  
Author(s):  
Cila Blatt ◽  
Melvin L. DePamphills
Keyword(s):  
Transcription Enhancer ◽  
Enhancer Factor

scholarly journals High Cancer-Specific Expression of Mesothelin (MSLN) Is Attributable to an Upstream Enhancer Containing a Transcription Enhancer Factor–Dependent MCAT Motif

2007 ◽  
Vol 67 (19) ◽  
pp. 9055-9065 ◽  
Author(s):  
Tomas Hucl ◽  
Jonathan R. Brody ◽  
Eike Gallmeier ◽  
Christine A. Iacobuzio-Donahue ◽  
Iain K. Farrance ◽  
...  
Keyword(s):  
Specific Expression ◽  
Transcription Enhancer ◽  
Enhancer Factor

scholarly journals DTEF-1, a Novel Member of the Transcription Enhancer Factor-1 (TEF-1) Multigene Family

1996 ◽  
Vol 271 (14) ◽  
pp. 8260-8265 ◽  
Author(s):  
Anthony Azakie ◽  
Sarah B. Larkin ◽  
Iain K. Farrance ◽  
Gabriele Grenningloh ◽  
Charles P. Ordahl
Keyword(s):  
Multigene Family ◽  
Transcription Enhancer ◽  
Enhancer Factor
Sign in / Sign up

Export Citation Format

Share Document