User:Wayne Decatur/Gal 4
From Proteopedia
m |
m |
||
| Line 12: | Line 12: | ||
==DNA Recognition by Gal4p== | ==DNA Recognition by Gal4p== | ||
| + | <scene name='70/701975/1d66_firstglance_secondary/2'>Each monomer of the dimer is made of 3 alpha helices</scene>. | ||
| + | |||
| + | <blockquote><big> | ||
| + | STRUCTURE KEY: | ||
| + | {{Template:ColorKey_Helix}}, | ||
| + | {{Template:ColorKey_Strand}}, | ||
| + | {{Template:ColorKey_Turn}}. | ||
| + | </big></blockquote> | ||
The protein <scene name='70/701975/1d66_firstglance/2'>binds as a dimer to a symmetrical 17-base-pair sequence</scene>. Specifically, the consensus Gal4p-binding site is a 17-mer of sequence conforming to the motif below.<br> | The protein <scene name='70/701975/1d66_firstglance/2'>binds as a dimer to a symmetrical 17-base-pair sequence</scene>. Specifically, the consensus Gal4p-binding site is a 17-mer of sequence conforming to the motif below.<br> | ||
| Line 30: | Line 38: | ||
<ref group="xtra">PMID:1557122</ref><references group="xtra"/> | <ref group="xtra">PMID:1557122</ref><references group="xtra"/> | ||
| - | == | + | ==See Also== |
* [[Gal3-Gal80-Gal4]] | * [[Gal3-Gal80-Gal4]] | ||
Revision as of 18:11, 12 May 2015
Gal4p is a transcriptional activator in Saccharomyces cerevisiae that regulates the expression of genes to coordinate the response to the carbon source galactose.
|
Contents |
Background
Gal4p is a transcriptional activator in Saccharomyces cerevisiae that regulates the expression of genes to coordinate the response to the carbon source galactose. Gal4p is an 881-amino-acid protein with a Zn cluster-type DNA-binding domain, a linker domain, a dimerization domain, and two acidic activation domains. The structure of the DNA-binding domain(1d66), the dimerization domain (1hbw), and the activation domain (3bts) has been solved separately. There is a structure of the DNA-binding and dimerization domains as one unit as well (3coq).
Pioneering studies on Gal4p from the Ptashne laboratory shaped our understanding of eukaryotic transcriptional activation, and Gal4p derivatives, along with their cognate promoters, continue to be used as tools by investigators preforming research in yeast.
DNA Recognition by Gal4p
.
STRUCTURE KEY: Alpha Helices, Beta Strands , Turns.
The protein . Specifically, the consensus Gal4p-binding site is a 17-mer of sequence conforming to the motif below.
5'-CGGNNNNNNNNNNNCCG-3'
|||||||||||||||||
3'-CGGNNNNNNNNNNNGGC-5'
The DNA binding domain . (In the crystal structure 1d66, the zinc ions are actually represented by other members of the same group on the periodic table, the heavier cadmium ions.) The Zn-binding motif lets the structure accomplish more with fewer amino acids, the metals lending an "economy of structure", arranging two small helices to recognize a specific DNA site.
A C G T
The third large helix of each dimer subunit interacts with the other . Note the abundance of gray residues in the central stem protruding from a site roughly the center of the DNA binding site. The dimer interface is more fully explored in a later publication with an expanded structure, see 3coq.
Reference
- Marmorstein R, Carey M, Ptashne M, Harrison SC. DNA recognition by GAL4: structure of a protein-DNA complex. Nature. 1992 Apr 2;356(6368):408-14. PMID:1557122 doi:http://dx.doi.org/10.1038/356408a0
