Localization of a site for interaction with hepatic male-specific proteins in two rat estrogen sulfotransferase genes.
Using electromobility shift assay the interaction of fragments of two paralogous rat estrogen sulfotransferase (Ste) genes with proteins of nuclear extracts from male and female rat liver was studied. Male-specific DNA-protein complexes were revealed with labeled oligonucleotides corresponding to fragments +1150/+1449, +1358/+1449, +1397/+1449, and +1417/+1449 of intron 1 of the Ste1 gene. The removal of a 20 bp region corresponding to the sequence +1430/+1449, or even either 5;- or 3;-terminal 5 bp of this region abolished the selective interaction of the oligonucleotides with the male-specific protein(s). According to the results of the experiments on mutual competition of the oligonucleotides, the fragment of the Ste2 gene corresponding to the sequence +1397/+1449 of the Ste1 gene formed complexes with the same male-specific protein(s) as the fragment of the Ste1 gene did. The data suggest the mapped element to participate in gender differentiation of the expression of the Ste1 and Ste2 genes.
Astapova
I I
II
Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, 119991, Russia.
Shchelkunova
T A
TA
Morozov
I A
IA
Smirnov
A N
AN
Rubtsov
P M
PM
D000818:Animals; D001483:Base Sequence; D001665:Binding Sites / Q000235:genetics; D001667:Binding, Competitive; D024202:Electrophoretic Mobility Shift Assay; D005260:Female; D008099:Liver / Q000378:metabolism*; D008297:Male; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000378:metabolism*; D009841:Oligonucleotides / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding; D051381:Rats; D012689:Sequence Homology, Nucleic Acid; D012737:Sex Factors; D015238:Sulfotransferases / Q000235:genetics* / Q000378:metabolism
D009687:Nuclear Proteins; D009841:Oligonucleotides; D015238:Sulfotransferases; C020122:estrone sulfotransferase