On the nature of rat hepatic and mouse olfactory sulfotransferases

Chem Biol Interact. 1998 Feb 20;109(1-3):69-80. doi: 10.1016/s0009-2797(97)00121-x.

Abstract

Rat hydroxysteroid sulfotransferase (HS-SULT) cDNAs, ST-40 and ST-20 are 90% identical in amino acid sequences and show different substrate specificities toward dehydroepiandrosterone (DHEA), androsterone (AD) and cortisol (CS). ST-40 enzyme is active toward the three substrates, whereas ST-20 enzyme is preferentially active for CS. First we prepared mutants of well conserved histidine, lysine and asparagine by site-directed mutagenesis. Secondly we constructed 20 chimeric HS-SULTs by reciprocal exchange of five protein domains between ST-20 and ST-40 enzymes. The studies on the expressed mutant and chimeric enzymes indicate the importance of the C-terminal region for the substrate specificity and the involvement of multiple regions for the enzyme activities. Next we determined the genetic loci of ST-40 and ST-20 by fluorescence in situ hybridization. Biotinylated ST-20 and ST-40 probes gave a pair of fluorescent spots on the same region of rat chromosome 1 and the loci of these genes were localized to the same chromosomal region of 1q21.3 --> q22.1. Finally we studied mouse olfactory phenol SULT (P-SULT). It was immunolocalized in the cytoplasm of mouse olfactory sustentacular cells and mouse nasal cytosols show high SULT activities toward phenolic aromatic odorants. We subsequently isolated a mouse P-SULT cDNA from mouse olfactory cDNA library. It encodes 304 amino acid polypeptide and is 94% identical with rat ST1C1 in amino acid sequences.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Arylsulfotransferase / genetics*
  • DNA, Complementary / genetics
  • Liver / enzymology*
  • Mice
  • Molecular Sequence Data
  • Olfactory Pathways / enzymology*
  • Rats
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Sequence Homology, Amino Acid
  • Sulfotransferases / genetics*

Substances

  • DNA, Complementary
  • Recombinant Fusion Proteins
  • Sulfotransferases
  • Arylsulfotransferase
  • alcohol sulfotransferase