Photocontrol of DNA Binding Specificity of a Miniature Engrailed Homeodomain

2005 ◽  
Vol 127 (44) ◽  
pp. 15624-15629 ◽  
Author(s):  
Lucia Guerrero ◽  
Oliver S. Smart ◽  
G. Andrew Woolley ◽  
Rudolf K. Allemann
Keyword(s):  
Dna Binding ◽  
Binding Specificity ◽  
Dna Binding Specificity ◽  
Engrailed Homeodomain

The DNA binding specificity of engrailed homeodomain

1998 ◽  
Vol 276 (3) ◽  
pp. 529-536 ◽  
Author(s):  
Alexandra Draganescu ◽  
Thomas D. Tullius
Keyword(s):  
Dna Binding ◽  
Binding Specificity ◽  
Dna Binding Specificity ◽  
Engrailed Homeodomain

scholarly journals DNA-binding specificity of GATA family transcription factors.

1993 ◽  
Vol 13 (7) ◽  
pp. 3999-4010 ◽  
Author(s):  
M Merika ◽  
S H Orkin
Keyword(s):  
Transcription Factors ◽  
Dna Binding ◽  
Mammalian Cells ◽  
Chimeric Protein ◽  
Binding Specificity ◽  
Mobility Shift ◽  
Binding Domains ◽  
Dna Binding Specificity ◽  
Mobility Shift Assay ◽  
Gata Family

GATA-binding proteins constitute a family of transcription factors that recognize a target site conforming to the consensus WGATAR (W = A or T and R = A or G). Here we have used the method of polymerase chain reaction-mediated random site selection to assess in an unbiased manner the DNA-binding specificity of GATA proteins. Contrary to our expectations, we show that GATA proteins bind a variety of motifs that deviate from the previously assigned consensus. Many of the nonconsensus sequences bind protein with high affinity, equivalent to that of conventional GATA motifs. By using the selected sequences as probes in the electrophoretic mobility shift assay, we demonstrate overlapping, but distinct, sequence preferences for GATA family members, specified by their respective DNA-binding domains. Furthermore, we provide additional evidence for interaction of amino and carboxy fingers of GATA-1 in defining its binding site. By performing cotransfection experiments, we also show that transactivation parallels DNA binding. A chimeric protein containing the finger domain of areA and the activation domains of GATA-1 is capable of activating transcription in mammalian cells through GATA motifs. Our findings suggest a mechanism by which GATA proteins might selectively regulate gene expression in cells in which they are coexpressed.

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