Cross-binding of factors to functionally different promoter elements in c-fos and skeletal actin genes

1989 ◽  
Vol 9 (5) ◽  
pp. 2191-2201
Author(s):  
K Walsh
Keyword(s):  
Serum Response Factor ◽  
Regulatory Element ◽  
Specific Expression ◽  
Tissue Specific ◽  
Tissue Specific Expression ◽  
Actin Genes ◽  
Tata Element ◽  
Actin Promoter ◽  
Serum Response

A conserved 28-base-pair element in the skeletal actin promoter was sufficient to activate muscle-specific expression when placed upstream of a TATA element. This muscle regulatory element (MRE) is similar in structure to the serum response element (SRE), which is present in the promoters of the c-fos proto-oncogene and the nonmuscle actin genes. The SRE can function as a constitutive promoter element. Though the MRE and SRE differed in their tissue-specific expression properties, both elements bound to the same protein factors in vitro. These proteins are the serum response factor (SRF) and the muscle actin promoter factors 1 and 2 (MAPF1 and MAPF2). The SRF and MAPF proteins were resolved by chromatographic procedures, and they differed in their relative affinities for each element. The factors were further distinguished by their distinct, but overlapping, methylation interference footprint patterns on each element. These data indicate that the differences in tissue-specific expression may be due to a complex interaction of protein factors with these sequences.

scholarly journals Cross-binding of factors to functionally different promoter elements in c-fos and skeletal actin genes.

1989 ◽  
Vol 9 (5) ◽  
pp. 2191-2201 ◽  
Author(s):  
K Walsh
Keyword(s):  
Serum Response Factor ◽  
Regulatory Element ◽  
Specific Expression ◽  
Tissue Specific ◽  
Tissue Specific Expression ◽  
Actin Genes ◽  
Tata Element ◽  
Actin Promoter ◽  
Serum Response

A conserved 28-base-pair element in the skeletal actin promoter was sufficient to activate muscle-specific expression when placed upstream of a TATA element. This muscle regulatory element (MRE) is similar in structure to the serum response element (SRE), which is present in the promoters of the c-fos proto-oncogene and the nonmuscle actin genes. The SRE can function as a constitutive promoter element. Though the MRE and SRE differed in their tissue-specific expression properties, both elements bound to the same protein factors in vitro. These proteins are the serum response factor (SRF) and the muscle actin promoter factors 1 and 2 (MAPF1 and MAPF2). The SRF and MAPF proteins were resolved by chromatographic procedures, and they differed in their relative affinities for each element. The factors were further distinguished by their distinct, but overlapping, methylation interference footprint patterns on each element. These data indicate that the differences in tissue-specific expression may be due to a complex interaction of protein factors with these sequences.

Functional antagonism between YY1 and the serum response factor

1992 ◽  
Vol 12 (9) ◽  
pp. 4209-4214
Author(s):  
A Gualberto ◽  
D LePage ◽  
G Pons ◽  
S L Mader ◽  
K Park ◽  
...  
Keyword(s):  
Serum Response Factor ◽  
Regulatory Element ◽  
Target Sequence ◽  
Response Factor ◽  
Basal Expression ◽  
Actin Promoter ◽  
Alpha Actin ◽  
Serum Response

The rapid, transient induction of the c-fos proto-oncogene by serum growth factors is mediated by the serum response element (SRE). The SRE shares homology with the muscle regulatory element (MRE) of the skeletal alpha-actin promoter. It is not known how these elements respond to proliferative and cell-type-specific signals, but the response appears to involve the binding of the serum response factor (SRF) and other proteins. Here, we report that YY1, a multifunctional transcription factor, binds to SRE and MRE sequences in vitro. The methylation interference footprint of YY1 overlaps with that of the SRF, and YY1 competes with the SRF for binding to these DNA elements. Overexpression of YY1 repressed serum-inducible and basal expression from the c-fos promoter and repressed basal expression from the skeletal alpha-actin promoter. YY1 also repressed expression from the individual SRE and MRE sequences upstream from a TATA element. Unlike that of YY1, SRF overexpression alone did not influence the transcriptional activity of the target sequence, but SRF overexpression could reverse YY1-mediated trans repression. These data suggest that YY1 and the SRF have antagonistic functions in vivo.

scholarly journals Functional antagonism between YY1 and the serum response factor.

1992 ◽  
Vol 12 (9) ◽  
pp. 4209-4214 ◽  
Author(s):  
A Gualberto ◽  
D LePage ◽  
G Pons ◽  
S L Mader ◽  
K Park ◽  
...  
Keyword(s):  
Serum Response Factor ◽  
Regulatory Element ◽  
Target Sequence ◽  
Response Factor ◽  
Basal Expression ◽  
Actin Promoter ◽  
Alpha Actin ◽  
Serum Response

The rapid, transient induction of the c-fos proto-oncogene by serum growth factors is mediated by the serum response element (SRE). The SRE shares homology with the muscle regulatory element (MRE) of the skeletal alpha-actin promoter. It is not known how these elements respond to proliferative and cell-type-specific signals, but the response appears to involve the binding of the serum response factor (SRF) and other proteins. Here, we report that YY1, a multifunctional transcription factor, binds to SRE and MRE sequences in vitro. The methylation interference footprint of YY1 overlaps with that of the SRF, and YY1 competes with the SRF for binding to these DNA elements. Overexpression of YY1 repressed serum-inducible and basal expression from the c-fos promoter and repressed basal expression from the skeletal alpha-actin promoter. YY1 also repressed expression from the individual SRE and MRE sequences upstream from a TATA element. Unlike that of YY1, SRF overexpression alone did not influence the transcriptional activity of the target sequence, but SRF overexpression could reverse YY1-mediated trans repression. These data suggest that YY1 and the SRF have antagonistic functions in vivo.

scholarly journals Identification of an Intronic Regulatory Element Necessary for Tissue-Specific Expression of Foxn1 in Thymic Epithelial Cells

2019 ◽  
Vol 203 (3) ◽  
pp. 686-695 ◽  
Author(s):  
Brian M. Larsen ◽  
Jennifer E. Cowan ◽  
Yueqiang Wang ◽  
Yu Tanaka ◽  
Yongge Zhao ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Regulatory Element ◽  
Thymic Epithelial Cells ◽  
Specific Expression ◽  
Tissue Specific ◽  
Tissue Specific Expression

scholarly journals A compact, in vivo screen of all 6-mers reveals drivers of tissue-specific expression and guides synthetic regulatory element design

2013 ◽  
Vol 14 (7) ◽  
pp. R72 ◽  
Author(s):  
Robin P Smith ◽  
Samantha J Riesenfeld ◽  
Alisha K Holloway ◽  
Qiang Li ◽  
Karl K Murphy ◽  
...  
Keyword(s):  
Regulatory Element ◽  
Specific Expression ◽  
Tissue Specific ◽  
Tissue Specific Expression ◽  
In Vivo Screen

scholarly journals SRF protein is upregulated during stretch-induced hypertrophy of rooster ALD muscle

1999 ◽  
Vol 86 (6) ◽  
pp. 1793-1799 ◽  
Author(s):  
Martin Flück ◽  
James A. Carson ◽  
Robert J. Schwartz ◽  
Frank W. Booth
Keyword(s):  
Skeletal Muscle ◽  
Transcription Factor ◽  
Protein Concentration ◽  
Serum Response Factor ◽  
Regulatory Element ◽  
Left Wing ◽  
Serum Response Element ◽  
Response Element ◽  
Actin Promoter ◽  
Serum Response

Serum response element 1 has previously been reported to be necessary and sufficient for activation of the skeletal α-actin promoter during hypertrophy of the anterior latissimus dorsi (ALD) muscle of roosters [J. A. Carson, R. J. Schwartz, and F. W. Booth. Am. J. Physiol. 270 ( Cell Physiol. 39): C1624–C1633, 1996]. Serum response factor (SRF) protein is the transcription factor that binds as a homodimer to serum response element 1 and activates the skeletal α-actin promoter. An increased expression of exogenous SRF protein in replicating C2C12myoblasts induced a three- to fourfold activation of the skeletal α-actin promoter (L. Wei, W. Zhou, J. D. Croissant, F.-E. Johansen, R. Prywes, A. Balasubramamyan, and R. J. Schwartz. J. Biol. Chem. 273: 30287–30294, 1998). Thus we hypothesized that SRF protein concentration would be increased during hypertrophy of skeletal muscle. In the present study, 10% of the rooster’s body weight was attached to the left wing to induce enlargement of the ALD muscle compared with the contralateral muscle. With Western analysis, a significant increase in SRF protein per gram of wet weight of the ALD muscle was noted at 7 and 13 days of hypertrophy. Furthermore, the increase in SRF protein occurred in both crude nuclear protein and cytoplasmic fractions in 7-day stretched ALD muscles. This is the first report showing increased protein concentration for a transcription factor whose regulatory element in the skeletal α-actin promoter has previously been shown to be required for the transduction of a hypertrophy signal in overloaded skeletal muscle of an animal.

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