Molecular cloning and expression of an amine sulfotransferase cDNA: A new gene family of cytosolic sulfotransferases in mammals

Kouichi Yoshinari, Kiyoshi Nagata, Makoto Ogino, Ken Ichi Fujita, Toshifumi Shiraga, Kazuhide Iwasaki, Takehisa Hata, Yasushi Yamazoe

Research output: Contribution to journalArticlepeer-review

34 Citations (Scopus)

Abstract

A cDNA of amine sulfotransferase-RB1 (AST-RB1), which efficiently catalyzes 4-phenyl-1,2,3,6-tetrahydropyridine (PTHP) sulfation, has been isolated by immunoscreening of a rabbit liver cDNA library. The cDNA consisted of 1117 base pairs and encoded a protein of 301 amino acids with a molecular weight of 35,876. The deduced amino acid sequence matched at six positions those of peptide fragments obtained from purified AST-RB1 protein. The sequence had less than 38% identity at the amino acid level with cytosolic sulfotransferases in mammals, although high degrees of similarity were observed with regions conserved throughout mammalian sulfotransferases. These results indicate that AST-RB1, arbitrarily named sulfotransferase 3A1 (ST3A1), constitutes a new and third gene family of cytosolic sulfotransferases in mammals. ST3A1 expressed in Escherichia coli as a fused protein catalyzed sulfation of amines such as PTHP, aniline, 4-chloroaniline, 2-naphthylamine, and desipramine, but barely O-sulfation of typical aryl and hydroxysteroid sulfotransferase substrates. These data unequivocally demonstrate the existence of a cytosolic sulfotransferase showing a high selectivity for amine substrates, and indicate that multiple forms of sulfotransferase mediate sulfation of xenobiotics in mammalian livers.

Original languageEnglish
Pages (from-to)479-486
Number of pages8
JournalJournal of biochemistry
Volume123
Issue number3
DOIs
Publication statusPublished - 1998 Mar

Keywords

  • Amino compound
  • Bacterial expression
  • Rabbit
  • Sulfotransferase
  • cDNA

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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