Nucleic Acids Research, Vol 26, Issue 11 2672-2678, Copyright © 1998 by Oxford University Press
RC Wilkins and JT Lis
GAGA transcription factor (GAF) is an essential protein in Drosophila ,
important for the transcriptional regulation of numerous genes. GAF binds
to GA repeats in the promoters of these genes via a DNA-binding domain
containing a single zinc finger. While GAF binding sites are typically
composed of 3.5 GA repeats, the Drosophila hsp70 gene contains much smaller
elements, some of which are as little as three bases (GAG) in length.
Interestingly, the binding of GAF to more distant trinucleotide elements is
relatively strong and not appreciably affected by the removal of larger GA
arrays in the promoter. Moreover, a simple synthetic GAG sequence is
sufficient to bind GAF in vitro . Here we directly compare the affinity of
GAF for different sequence elements by immunoprecipitation and gel mobility
shift analysis. Furthermore, our measures of the concentration of GAF in
vivo indicate that it is a highly abundant nuclear protein, prevalent
enough to occupy a sizable fraction of correspondingly abundant
trinucleotide sites.
ARTICLES
GAGA factor binding to DNA via a single trinucleotide sequence element
Section of Genetics and Development, Cornell University, Ithaca, NY 14853, USA.
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