Human sulfotransferases SULT1C1 and SULT1C2: cDNA characterization, gene cloning, and chromosomal localization

Robert Freimuth, Rebecca B. Raftogianis, Thomas C. Wood, Eunpyo Moon, Ung Jin Kim, Jingping Xu, Michael J. Siciliano, Richard M Weinshilboum

Research output: Contribution to journalArticle

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Abstract

Sulfate conjugation catalyzed by sulfotransferase (SULT) enzymes is an important pathway in the biotransformation of many drugs, other xenobiotics, neurotransmitters, and hormones. We previously described a human cDNA, SULT1C1, that encoded a protein similar in sequence to that of rat ST1C1. Subsequently, a related human cDNA, SULT1C2, was reported. In the present study, we set out to characterize further the human SULT1C1 cDNA and then to clone, structurally characterize, and map its gene. As an initial step, we performed 5'- and 3'-RACE with SULT1C1 cDNA. Those experiments demonstrated that a small number of SULTIC1 transcripts contained an 'insert,' which we later showed resulted from alternative splicing that involved an Alu sequence in intron 3 of SULT1C1. We then cloned and structurally characterized the SULT1C1 gene from a human genomic BAC library. Because the sequence of SULT1C2 was closely related to that of SULT1C1 and because the genes for other human SULT paralogues occur in clusters, we screened the BAC clones that had been positive for SULT1C1 to search for SULT1C2 and discovered a clone that contained both genes. That BAC was used to sequence and structurally characterize SULT1C2. SULT1C1 and SULT1C2 were approximately 21 and 10 kb in length, respectively. Both genes contained seven exons that encoded protein, and both had structures that were similar to those of other genes that encode members of the SULT1 family. Finally, human SULT1C1 and SULT1C2 mapped to 2q11.2 by fluorescence in situ hybridization. The cloning and structural characterization of SULT1C1 and SULT1C2 will now make it possible to perform molecular genetic and pharmacogenomic studies of these sulfate-conjugating enzymes in humans. (C) 2000 Academic Press.

Original languageEnglish (US)
Pages (from-to)157-165
Number of pages9
JournalGenomics
Volume65
Issue number2
DOIs
StatePublished - Apr 15 2000

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Sulfotransferases
Organism Cloning
Complementary DNA
Genes
Clone Cells
Sulfates
N-hydroxy-2-acetylaminofluorene sulfotransferase
Genomic Library
Alternative Splicing
Xenobiotics
Enzymes
Biotransformation
Fluorescence In Situ Hybridization
Introns
Neurotransmitter Agents
Molecular Biology
Exons
Proteins
Hormones

ASJC Scopus subject areas

  • Genetics

Cite this

Human sulfotransferases SULT1C1 and SULT1C2 : cDNA characterization, gene cloning, and chromosomal localization. / Freimuth, Robert; Raftogianis, Rebecca B.; Wood, Thomas C.; Moon, Eunpyo; Kim, Ung Jin; Xu, Jingping; Siciliano, Michael J.; Weinshilboum, Richard M.

In: Genomics, Vol. 65, No. 2, 15.04.2000, p. 157-165.

Research output: Contribution to journalArticle

Freimuth, Robert ; Raftogianis, Rebecca B. ; Wood, Thomas C. ; Moon, Eunpyo ; Kim, Ung Jin ; Xu, Jingping ; Siciliano, Michael J. ; Weinshilboum, Richard M. / Human sulfotransferases SULT1C1 and SULT1C2 : cDNA characterization, gene cloning, and chromosomal localization. In: Genomics. 2000 ; Vol. 65, No. 2. pp. 157-165.
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abstract = "Sulfate conjugation catalyzed by sulfotransferase (SULT) enzymes is an important pathway in the biotransformation of many drugs, other xenobiotics, neurotransmitters, and hormones. We previously described a human cDNA, SULT1C1, that encoded a protein similar in sequence to that of rat ST1C1. Subsequently, a related human cDNA, SULT1C2, was reported. In the present study, we set out to characterize further the human SULT1C1 cDNA and then to clone, structurally characterize, and map its gene. As an initial step, we performed 5'- and 3'-RACE with SULT1C1 cDNA. Those experiments demonstrated that a small number of SULTIC1 transcripts contained an 'insert,' which we later showed resulted from alternative splicing that involved an Alu sequence in intron 3 of SULT1C1. We then cloned and structurally characterized the SULT1C1 gene from a human genomic BAC library. Because the sequence of SULT1C2 was closely related to that of SULT1C1 and because the genes for other human SULT paralogues occur in clusters, we screened the BAC clones that had been positive for SULT1C1 to search for SULT1C2 and discovered a clone that contained both genes. That BAC was used to sequence and structurally characterize SULT1C2. SULT1C1 and SULT1C2 were approximately 21 and 10 kb in length, respectively. Both genes contained seven exons that encoded protein, and both had structures that were similar to those of other genes that encode members of the SULT1 family. Finally, human SULT1C1 and SULT1C2 mapped to 2q11.2 by fluorescence in situ hybridization. The cloning and structural characterization of SULT1C1 and SULT1C2 will now make it possible to perform molecular genetic and pharmacogenomic studies of these sulfate-conjugating enzymes in humans. (C) 2000 Academic Press.",
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AU - Moon, Eunpyo

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AU - Siciliano, Michael J.

AU - Weinshilboum, Richard M

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AB - Sulfate conjugation catalyzed by sulfotransferase (SULT) enzymes is an important pathway in the biotransformation of many drugs, other xenobiotics, neurotransmitters, and hormones. We previously described a human cDNA, SULT1C1, that encoded a protein similar in sequence to that of rat ST1C1. Subsequently, a related human cDNA, SULT1C2, was reported. In the present study, we set out to characterize further the human SULT1C1 cDNA and then to clone, structurally characterize, and map its gene. As an initial step, we performed 5'- and 3'-RACE with SULT1C1 cDNA. Those experiments demonstrated that a small number of SULTIC1 transcripts contained an 'insert,' which we later showed resulted from alternative splicing that involved an Alu sequence in intron 3 of SULT1C1. We then cloned and structurally characterized the SULT1C1 gene from a human genomic BAC library. Because the sequence of SULT1C2 was closely related to that of SULT1C1 and because the genes for other human SULT paralogues occur in clusters, we screened the BAC clones that had been positive for SULT1C1 to search for SULT1C2 and discovered a clone that contained both genes. That BAC was used to sequence and structurally characterize SULT1C2. SULT1C1 and SULT1C2 were approximately 21 and 10 kb in length, respectively. Both genes contained seven exons that encoded protein, and both had structures that were similar to those of other genes that encode members of the SULT1 family. Finally, human SULT1C1 and SULT1C2 mapped to 2q11.2 by fluorescence in situ hybridization. The cloning and structural characterization of SULT1C1 and SULT1C2 will now make it possible to perform molecular genetic and pharmacogenomic studies of these sulfate-conjugating enzymes in humans. (C) 2000 Academic Press.

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