Engineering the Loop Region of a Homeodomain-Leucine Zipper Protein Promotes Efficient Binding to a Monomeric DNA Binding Site†

Biochemistry ◽  
2004 ◽  
Vol 43 (50) ◽  
pp. 15845-15851 ◽  
Author(s):  
Adriana E. Tron ◽  
Elina Welchen ◽  
Daniel H. Gonzalez
Keyword(s):  
Dna Binding ◽  
Binding Site ◽  
Leucine Zipper ◽  
Loop Region ◽  
Dna Binding Site ◽  
Leucine Zipper Protein

Sequence-specific transcriptional activation by Myc and repression by Max

1993 ◽  
Vol 13 (1) ◽  
pp. 383-390
Author(s):  
C Amin ◽  
A J Wagner ◽  
N Hay
Keyword(s):  
Dna Binding ◽  
Binding Site ◽  
Transcriptional Activation ◽  
Transcriptional Repression ◽  
Leucine Zipper ◽  
Cellular Proliferation ◽  
Helix Loop Helix ◽  
Dna Binding Site ◽  
Carboxy Terminal

The c-Myc oncoprotein, which is required for cellular proliferation, resembles in its structure a growing number of transcription factors. However, the mechanism of its action in vivo is not yet clear. The discovery of the specific cognate DNA-binding site for Myc and its specific heterodimerization partner, Max, enabled the use of direct experiments to elucidate how Myc functions in vivo and how this function is modulated by Max. Here we demonstrate that exogenously expressed Myc is capable of activating transcription in vivo through its specific DNA-binding site. Moreover, transcriptional activation by Myc is dependent on the basic region, the integrity of the helix-loop-helix and leucine zipper dimerization motifs located in the carboxy-terminal portion of the protein, and the regions in the amino terminus conserved among Myc family proteins. In contrast to Myc, exogenously expressed Max elicited transcriptional repression and blocked transcriptional activation by Myc through the same DNA-binding site. Our results suggest a functional antagonism between Myc and Max which is mediated by their relative levels in the cells. A model for the activity of Myc and Max in vivo is presented.

scholarly journals Sequence-specific transcriptional activation by Myc and repression by Max.

1993 ◽  
Vol 13 (1) ◽  
pp. 383-390 ◽  
Author(s):  
C Amin ◽  
A J Wagner ◽  
N Hay
Keyword(s):  
Dna Binding ◽  
Binding Site ◽  
Transcriptional Activation ◽  
Transcriptional Repression ◽  
Leucine Zipper ◽  
Cellular Proliferation ◽  
Helix Loop Helix ◽  
Dna Binding Site ◽  
Carboxy Terminal

The c-Myc oncoprotein, which is required for cellular proliferation, resembles in its structure a growing number of transcription factors. However, the mechanism of its action in vivo is not yet clear. The discovery of the specific cognate DNA-binding site for Myc and its specific heterodimerization partner, Max, enabled the use of direct experiments to elucidate how Myc functions in vivo and how this function is modulated by Max. Here we demonstrate that exogenously expressed Myc is capable of activating transcription in vivo through its specific DNA-binding site. Moreover, transcriptional activation by Myc is dependent on the basic region, the integrity of the helix-loop-helix and leucine zipper dimerization motifs located in the carboxy-terminal portion of the protein, and the regions in the amino terminus conserved among Myc family proteins. In contrast to Myc, exogenously expressed Max elicited transcriptional repression and blocked transcriptional activation by Myc through the same DNA-binding site. Our results suggest a functional antagonism between Myc and Max which is mediated by their relative levels in the cells. A model for the activity of Myc and Max in vivo is presented.

scholarly journals Determinants for DNA-binding site recognition by the glucocorticoid receptor.

1992 ◽  
Vol 267 (35) ◽  
pp. 24941-24947
Author(s):  
J Zilliacus ◽  
A.P. Wright ◽  
U Norinder ◽  
J.A. Gustafsson ◽  
J Carlstedt-Duke
Keyword(s):  
Dna Binding ◽  
Glucocorticoid Receptor ◽  
Binding Site ◽  
Dna Binding Site ◽  
Site Recognition
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