Synthesis of the basic-helix-loop-helix region of the immunoglobulin enhancer binding protein E47 and evaluation of its structural and DNA binding properties

2009 ◽  
Vol 46 (2) ◽  
pp. 149-154 ◽  
Author(s):  
PATRICIA BISHOP ◽  
CORY JONES ◽  
INDRANEEL GHOSH ◽  
JEAN CHMIELEWSKI
2018 ◽  
Vol 28 (4) ◽  
pp. 484-496 ◽  
Author(s):  
Bradford H. Casey ◽  
Rahul K. Kollipara ◽  
Karine Pozo ◽  
Jane E. Johnson

1989 ◽  
Vol 9 (10) ◽  
pp. 4535-4540 ◽  
Author(s):  
H Beckmann ◽  
T Kadesch

We demonstrate that Saccharomyces cerevisiae cells possess a 33-41-kilodalton protein with DNA-binding properties remarkably similar to those of the immunoglobulin enhancer-binding protein NF-muE3. We further show that the muE3-binding site functions as an upstream activating sequence in yeast cells, stimulating transcription from a truncated CYC1 promoter. These data suggest that the yeast protein, designated YEB-3, and NF-muE3 are functionally related and perhaps evolutionarily conserved.


1989 ◽  
Vol 9 (10) ◽  
pp. 4535-4540
Author(s):  
H Beckmann ◽  
T Kadesch

We demonstrate that Saccharomyces cerevisiae cells possess a 33-41-kilodalton protein with DNA-binding properties remarkably similar to those of the immunoglobulin enhancer-binding protein NF-muE3. We further show that the muE3-binding site functions as an upstream activating sequence in yeast cells, stimulating transcription from a truncated CYC1 promoter. These data suggest that the yeast protein, designated YEB-3, and NF-muE3 are functionally related and perhaps evolutionarily conserved.


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