Genomic structure of rat liver aryl sulfotransferase IV-encoding gene

Khan, Akhtar S.; Taylor, Bryan R.; Chung, Keun Hee; Etheredge, Janet L.; Gonzales, Robert A.; Ringer, David P.

doi:10.1016/0378-1119(93)90028-2

Cited by 16 publications

(7 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…1). However, only one other ST gene structure has been reported, that of rat PST (Khan et al, 1993). The amino acid sequence encoded by the rat PST gene is only 38.8% identical to that of human DHEA ST, placing these two genes in separate "families" (Fig.…”

Section: Discussionmentioning

confidence: 97%

“…4). Unfortunately, the promoter region of the rat PST gene has not been reported (Khan et al, 1993), so no comparison can be made between promoters for the two genes. A protein more closely related to DHEA ST than rat PST is rat SMP2-a protein that, like DHEA ST, is classified structurally as a member of the HSST "family" (see Fig.…”

Section: Discussionmentioning

confidence: 99%

“…The only other ST gene structure reported to this time is that of a rat aryl or phenol ST (PST) gene, although the sequence of the promoter region for this gene was not reported (Khan et al, 1993). Even though the rat PST gene has seven introns rather than the five present in the STD gene, structures of the two genes show significant homology (Fig.…”

Section: Isolation Of Genomic Clones and Determination Of Exon-intronmentioning

confidence: 93%

“…Specifically, the lengths of exons III and IV in the STD gene are identical to those of exons V and VI in the rat PST gene, and the locations of splice junctions for those exons are conserved in the two genes (Fig. 4) (Khan et al, 1993) and partial structures of two rat SMP2 genes (Song et al, 1990). Positions of nucleotides in the corresponding cDNAs that are interrupted by introns are designated above splice junctions in the gene structure.…”

Section: Isolation Of Genomic Clones and Determination Of Exon-intronmentioning

confidence: 97%

See 3 more Smart Citations

Human Dehydroepiandrosterone Sulfotransferase Gene: Molecular Cloning and Structural Characterization

Otterness¹,

Her²,

Aksoy³

et al. 1995

DNA and Cell Biology

View full text Add to dashboard Cite

Dehydroepiandrosterone sulfotransferase (DHEA ST) catalyzes the sulfate conjugation of DHEA and other steroids. From 20 to 25% of subjects are included in a subgroup with high levels of hepatic DHEA ST activity, raising the possibility that this enzyme activity might be controlled by a genetic polymorphism. To understand the molecular mechanisms involved in regulating levels of DHEA ST activity in human tissue, we cloned the human DHEA ST gene, STD. STD spans at least 17 kb and is composed of 6 exons and 5 introns. The locations of the splice junctions for several of the introns are identical to those present in the rat phenol or aryl ST gene, the only other cytosolic ST gene for which the entire exon/intron structure has been reported, as well as those present in two partially characterized genes for the rat senescence marker protein, genes that are also thought to encode ST enzymes. The 5'-flanking region of the human STD gene does not contain canonical TATA or CCAAT elements, but this region is capable of promoting transcription of a reporter gene in Hep G2 cells. Molecular cloning and structural characterization of the human STD gene will make it possible to study genetic mechanisms involved in the regulation of DHEA ST activity in human tissue.

show abstract

Section: Discussionmentioning

confidence: 97%

Section: Discussionmentioning

confidence: 99%

Section: Isolation Of Genomic Clones and Determination Of Exon-intronmentioning

confidence: 93%

Section: Isolation Of Genomic Clones and Determination Of Exon-intronmentioning

confidence: 97%

See 2 more Smart Citations

Human Dehydroepiandrosterone Sulfotransferase Gene: Molecular Cloning and Structural Characterization

Otterness¹,

Her²,

Aksoy³

et al. 1995

DNA and Cell Biology

View full text Add to dashboard Cite

show abstract

“…Since our manuscript was submitted for publication, two additional sulfotransferase gene cloning papers (30,31) have come to our attention that are consistent with the 3'-terminal exon splice site involving the N-terminal glycine of the GXXGXXK P-loop motif.…”

mentioning

confidence: 97%

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.

View full text Add to dashboard Cite

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.

show abstract

Molecular mechanisms for the regulation of aryl sulfotransferase IV expression during 2-acetylaminofluorene-induced hepatocarcinogenesis in rat

Ringer

Yerokun

Khan

1994

Chemico-Biological Interactions

View full text Add to dashboard Cite

Genomic structure of rat liver aryl sulfotransferase IV-encoding gene

Cited by 16 publications

References 16 publications

Human Dehydroepiandrosterone Sulfotransferase Gene: Molecular Cloning and Structural Characterization

Human Dehydroepiandrosterone Sulfotransferase Gene: Molecular Cloning and Structural Characterization

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.

Molecular mechanisms for the regulation of aryl sulfotransferase IV expression during 2-acetylaminofluorene-induced hepatocarcinogenesis in rat

Contact Info

Product

Resources

About