Cloning and Sequence Analysis of the 5′-Flanking Region of the Estrogen Sulfotransferase Gene: Steroid Response Elements and Cell-Specific Nuclear DNA-Binding Proteins

Komatsu, Katsutoshi; Oeda, Toru; Strott, Charles A.

doi:10.1006/bbrc.1993.1965

Cited by 15 publications

(9 citation statements)

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“…The promoter region of the rat HST1 gene contains a canonical TATA box located 21 bp upstream of the cap site. Additionally, the 5'-flanking region contains steroid response element half-sites for GRE (TGTACA and TGTTCT) and ERE (TGACCT and AGGTCA); recall that similar motifs are present in the gpEST promoter (94). Although this is an interesting finding, it remains to be definitively determined, as in the case with gpEST, whether or not the steroid response element motifs present in the rat liver HST1 promoter region represent functional c/s-elements.…”

Section: B Hydroxysteroid Sulfotransferase (Hst)mentioning

confidence: 66%

“…Relatedly, cortisol is able to regulate the expression of the messenger for phenol sulfotransferase (enzymatic cousin of EST) in bovine bronchial epithelial cells (187). Thus, with these results in mind, the presence of steroid response element motifs in the promoter region of hEST (93) and gpEST (94) genes takes on an added degree of importance. Finally, nonsteroidal hormones, i.e.…”

Section: A Estrogen Sulfotransferasementioning

confidence: 99%

“…There is a sequence motif (TGACTCA) analogous to the binding site for the AP-1 family of transcription factors (jun/ fos) that confers phorbol ester inducibility through the action of protein kinase C (97). Block deletions of the gpEST 5'-flanking region indicate that basal promoter activity resides within the first 1000 bp upstream of the transcription initiation site; additional preliminary data from gel shift analyses demonstrate the presence of tissue-specific nuclear proteins interacting with 30 mer oligonucleotides containing either the ERE or GRE half-sites (94). Moreover, using a reporter gene construct, 17j3-estradiol, progesterone, cortisol, and testosterone induce promoter activity of gpEST in a dose-dependent manner, in contrast to the biologically inactive steroid metabolites pregnanolone and etiocholanolone, which have no effect (author's unpublished data).…”

Section: Transcriptional Regulationmentioning

confidence: 99%

“…As noted above, two members of this subfamily have had their 5'-flanking regions cloned; however, neither has been examined for promoter activity beyond a preliminary stage. For instance, sequence analysis of the 3-kb 5'-flanking region of the gpEST gene reveals a conventional TATA box variant (ATAAA) located 26 nt upstream of the cap site; additionally, there are sequences homologous to steroid response elements: two copies of an estrogen response element (ERE) half-site (AGGTCA) and one copy of a glucocorticoid response element (GRE) half-site (TGTTCT) (94). The AGGTCA sequence is also a shared motif related to members of the 'orphan' family of nuclear receptors, SF-1 and NGFI-B, transcription factors that coordinately regulate the expression of P 450 enzymes participating in the biosynthesis of steroids (95).…”

Section: Transcriptional Regulationmentioning

confidence: 99%

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Steroid Sulfotransferases

Strott¹

1996

Endocrine Reviews

162

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Section: B Hydroxysteroid Sulfotransferase (Hst)mentioning

confidence: 66%

Section: A Estrogen Sulfotransferasementioning

confidence: 99%

Section: Transcriptional Regulationmentioning

confidence: 99%

Section: Transcriptional Regulationmentioning

confidence: 99%

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Steroid Sulfotransferases

Strott¹

1996

Endocrine Reviews

162

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“…The genomic clones and the PCR product containing sequence not covered by the clones were sequenced by using the ATaq cycle sequencing kit (United States Biochemical) without subcloning. The DNA sequence for a 3-kb region covering the 5' flanking region of gpEST has been reported (8).…”

Section: Methodsmentioning

confidence: 99%

The 3'-terminal exon of the family of steroid and phenol sulfotransferase genes is spliced at the N-terminal glycine of the universally conserved GXXGXXK motif that forms the sulfonate donor binding site.

Chiba¹,

Komatsu²,

Lee³

et al. 1995

Proc. Natl. Acad. Sci. U.S.A.

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The guinea pig estrogen sulfotransferase gene has been cloned and compared to three other cloned steroid and phenol sulfotransferase genes (human estrogen sulfotransferase, human phenol sulfotransferase, and guinea pig 3av-hydroxysteroid sulfotransferase). The four sulfotransferase genes demonstrate a common outstanding feature: the splice sites for their 3'-terminal exons are identically located.That is, the 3'-terminal exon splice sites involve a glycine that constitutes the N-terminal glycine of an invariably conserved GXXGXXK motif present in all steroid and phenol sulfotransferases for which primary structures are known. This consistency strongly suggests that all steroid and phenol sulfotransferase genes will be similarly spliced. The GXXGXXK motif forms the active binding site for the universal sulfonate donor 3'-phosphoadenosine 5'-phosphosulfate. Amino acid sequence alignment of 19 cloned steroid and phenol sulfotransferases starting with the GXXGXXK motif indicates that the 3'-terminal exon for each steroid and phenol sulfotransferase gene encodes a similarly sized C-terminal fragment of the protein. Interestingly, on further analysis of the alignment, three distinct amino acid sequence patterns emerge. The presence of the conserved functional GXXGXXK motif suggests that the protein domains encoded by steroid and phenol sulfotransferase 3'-terminal exons have evolved from a common ancestor. Furthermnore, it is hypothesized that during the course of evolution, the 3'-terminal exon further diverged into at least three sulfotransferase subdivisions: a phenol or aryl group, an estrogen or phenolic steroid group, and a neutral steroid group.

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Retinoic acid inhibits hydrocortisone-stimulated expression of phenol sulfotransferase in bovine bronchial epithelial cells

Beckmann¹,

Palmatier²,

Kliewer³

1996

J. Cell. Physiol.

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The airway epithelium, which is commonly exposed to xenobiotics, contains the conjugative enzyme phenol sulfotransferase (PST). We have previously reported that hydrocortisone (HC) stimulates the expression of PST severalfold in cultured bovine bronchial epithelial cells (Beckmann et al., 1994, J. Cell. Physiol. 160:603-610). Here we report that this stimulation is attenuated by retinoic acid (RA). Dose-response measurements of both enzyme activities and mRNA levels indicated a 50% inhibition of HC-stimulated PST expression with 0.05 nM RA. Varied concentrations of RA had a general repressive effect on HC-stimulated PST expression, with no change in the half-maximal HC stimulatory concentration of 12.5 nM. Steady state kinetic measurements indicated no significant changes in apparent Km values of 3-5 microM for the acceptor substrate, 2-naphthol; only HC- and RA-dependent changes in Vmax were observed. These changes were likely due to altered enzyme expression, as evidenced by immunoblot and Northern blot hybridization analyses. Thus, the expression of PST within bronchial epithelial cells is not merely constitutive, but is subject to both positive and negative controls.

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Cloning and Sequence Analysis of the 5′-Flanking Region of the Estrogen Sulfotransferase Gene: Steroid Response Elements and Cell-Specific Nuclear DNA-Binding Proteins

Cited by 15 publications

References 0 publications

Steroid Sulfotransferases

Steroid Sulfotransferases

The 3'-terminal exon of the family of steroid and phenol sulfotransferase genes is spliced at the N-terminal glycine of the universally conserved GXXGXXK motif that forms the sulfonate donor binding site.

Retinoic acid inhibits hydrocortisone-stimulated expression of phenol sulfotransferase in bovine bronchial epithelial cells

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