scholarly journals A two-base change in a POU factor-binding site switches pituitary-specific to lymphoid-specific gene expression.

1990 ◽  
Vol 4 (1) ◽  
pp. 43-51 ◽  
Author(s):  
H P Elsholtz ◽  
V R Albert ◽  
M N Treacy ◽  
M G Rosenfeld
Keyword(s):  
Gene Expression ◽  
Binding Site ◽  
Base Change ◽  
Specific Gene ◽  
Factor Binding Site ◽  
Factor Binding ◽  
Specific Gene Expression

scholarly journals A new function for methyl CpG: Creating a C/EBPα binding site & mediating tissue‐specific gene expression

2010 ◽  
Vol 24 (S1) ◽  
Author(s):  
Raghunath Chatterjee ◽  
Vikas Rishi ◽  
Julian Rozenberg ◽  
Paramita Bhattacharya ◽  
Kimberly Glass ◽  
...  
Keyword(s):  
Gene Expression ◽  
Binding Site ◽  
Specific Gene ◽  
Tissue Specific ◽  
Tissue Specific Gene ◽  
Specific Gene Expression

scholarly journals The myosin light chain enhancer and the skeletal actin promoter share a binding site for factors involved in muscle-specific gene expression.

1991 ◽  
Vol 11 (7) ◽  
pp. 3735-3744 ◽  
Author(s):  
H Ernst ◽  
K Walsh ◽  
C A Harrison ◽  
N Rosenthal
Keyword(s):  
Gene Expression ◽  
Binding Site ◽  
Light Chain ◽  
Promoter Activity ◽  
Myosin Light Chain ◽  
Specific Gene ◽  
Sequence Motif ◽  
Factor Binding ◽  
Actin Promoter ◽  
Alpha Actin

The myosin light chain (MLC) 1/3 enhancer (MLC enhancer), identified at the 3' end of the skeletal MLC1/3 locus, contains a sequence motif that is homologous to a protein-binding site of the skeletal muscle alpha-actin promoter. Gel shift, competition, and footprint assays demonstrated that a CArG motif in the MLC enhancer binds the proteins MAPF1 and MAPF2, previously identified as factors interacting with the muscle regulatory element of the skeletal alpha-actin promoter. Transient transfection assays with constructs containing the chloramphenicol acetyltransferase reporter gene demonstrated that a 115-bp subfragment of the MLC enhancer is able to exert promoter activity when provided with a silent nonmuscle TATA box. A point mutation at the MAPF1/2-binding site interferes with factor binding and abolishes the promoter activity of the 115-bp fragment. The observation that an oligonucleotide encompassing the MAPF1/2 site of the MLC enhancer alone cannot serve as a promoter element suggests that additional factor-binding sites are necessary for this function. The finding that MAPF1 and MAPF2 recognize similar sequence motifs in two muscle genes, simultaneously activated during muscle differentiation, implies that these factors may have a role in coordinating the activation of contractile protein gene expression during myogenesis.

The myosin light chain enhancer and the skeletal actin promoter share a binding site for factors involved in muscle-specific gene expression

1991 ◽  
Vol 11 (7) ◽  
pp. 3735-3744
Author(s):  
H Ernst ◽  
K Walsh ◽  
C A Harrison ◽  
N Rosenthal
Keyword(s):  
Gene Expression ◽  
Binding Site ◽  
Light Chain ◽  
Promoter Activity ◽  
Myosin Light Chain ◽  
Specific Gene ◽  
Sequence Motif ◽  
Factor Binding ◽  
Actin Promoter ◽  
Alpha Actin

The myosin light chain (MLC) 1/3 enhancer (MLC enhancer), identified at the 3' end of the skeletal MLC1/3 locus, contains a sequence motif that is homologous to a protein-binding site of the skeletal muscle alpha-actin promoter. Gel shift, competition, and footprint assays demonstrated that a CArG motif in the MLC enhancer binds the proteins MAPF1 and MAPF2, previously identified as factors interacting with the muscle regulatory element of the skeletal alpha-actin promoter. Transient transfection assays with constructs containing the chloramphenicol acetyltransferase reporter gene demonstrated that a 115-bp subfragment of the MLC enhancer is able to exert promoter activity when provided with a silent nonmuscle TATA box. A point mutation at the MAPF1/2-binding site interferes with factor binding and abolishes the promoter activity of the 115-bp fragment. The observation that an oligonucleotide encompassing the MAPF1/2 site of the MLC enhancer alone cannot serve as a promoter element suggests that additional factor-binding sites are necessary for this function. The finding that MAPF1 and MAPF2 recognize similar sequence motifs in two muscle genes, simultaneously activated during muscle differentiation, implies that these factors may have a role in coordinating the activation of contractile protein gene expression during myogenesis.

scholarly journals The Role of Forkhead Box A2 to Restrict Androgen-Regulated Gene Expression of Lipocalin 5 in the Mouse Epididymis

2006 ◽  
Vol 20 (10) ◽  
pp. 2418-2431 ◽  
Author(s):  
Xiuping Yu ◽  
Kichiya Suzuki ◽  
Yongqing Wang ◽  
Aparna Gupta ◽  
Renjie Jin ◽  
...  
Keyword(s):  
Gene Expression ◽  
Transgenic Mice ◽  
Binding Site ◽  
Binding Sites ◽  
Transient Transfection ◽  
Specific Gene ◽  
Promoter Fragment ◽  
Specific Gene Expression ◽  
Principal Cells ◽  
Forkhead Box

Abstract Murine epididymal retinoic acid-binding protein [or lipocalin 5 (Lcn5)] is synthesized and secreted by the principal cells of the mouse middle/distal caput epididymidis. A 5-kb promoter fragment of the Lcn5 gene can dictate androgen-dependent and epididymis region-specific gene expression in transgenic mice. Here, we reported that the 1.8-kb Lcn5 promoter confers epididymis region-specific gene expression in transgenic mice. To decipher the mechanism that directs transcription, 14 chimeric constructs that sequentially removed 100 bp of 1.8-kb Lcn5 promoter were generated and transfected into epididymal cells and nonepididymal cells. Transient transfection analysis revealed that 1.3 kb promoter fragment gave the strongest response to androgens. Between the 1.2-kb to 1.3-kb region, two androgen receptor (AR) binding sites were identified. Adjacent to AR binding sites, a Foxa2 [Fox (Forkhead box) subclass A] binding site was confirmed by gel shift assay. Similar Foxa binding sites were also found on the promoters of human and rat Lcn5, indicating the Foxa binding site is conserved among species. We previously reported that among the three members of Foxa family, Foxa1 and Foxa3 were absent in the epididymis whereas Foxa2 was detected in epididymal principal cells. Here, we report that Foxa2 displays a region-specific expression pattern along the epididymis: no staining observed in initial segment, light staining in proximal caput, gradiently heavier staining in middle and distal caput, and strongest staining in corpus and cauda, regions with little or no expression of Lcn5. In transient transfection experiments, Foxa2 expression inhibits AR induction of the Lcn5 promoter, which is consistent with the lack of expression of Lcn5 in the corpus and cauda. We conclude that Foxa2 functions as a repressor that restricts AR regulation of Lcn5 to a segment-specific pattern in the epididymis.

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