Molecular cloning and expression of a cDNA encoding an olfactory-specific mouse phenol sulphotransferase

Biochem J. 1998 May 1;331 ( Pt 3)(Pt 3):953-8. doi: 10.1042/bj3310953.


Previously we demonstrated the presence of phenol sulphotransferase (P-ST) in mouse nasal cytosols and identified its zonal location in mouse nasal cavity by staining with an antiserum raised against a rat liver P-ST isoenzyme, PSTg. In the present study a cDNA was isolated from a mouse olfactory cDNA library by immunological screening with the antiserum. The isolated cDNA consisted of 1347 bp with a 912 bp open reading frame encoding a 304-residue polypeptide. Both the nucleotide and deduced amino acid sequences of the cDNA were 94% identical with those of a rat liver P-ST isoenzyme, ST1C1. The expressed enzyme in Escherichia coli displayed high P-ST activity towards phenolic odorants such as eugenol and guaiacol, and it showed a high N-hydroxy-2-acetylaminofluorene sulphation activity in comparison with the rat ST1C1 enzyme. These results indicate that the olfactory P-ST encoded by the cDNA is a mouse orthologue of rat ST1C1; however, expression of the olfactory P-ST mRNA is specific for nasal tissues as revealed by reverse transcriptase-mediated PCR (RT-PCR).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Arylsulfotransferase / chemistry*
  • Base Sequence
  • Cloning, Molecular
  • Escherichia coli / genetics
  • Eugenol / metabolism
  • Guaiacol / metabolism
  • Hydroxyacetylaminofluorene / metabolism
  • Kinetics
  • Mice
  • Molecular Sequence Data
  • Nasal Mucosa / enzymology*
  • Phylogeny
  • RNA, Messenger / metabolism
  • Recombinant Proteins / chemistry
  • Sequence Alignment
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid
  • Substrate Specificity


  • RNA, Messenger
  • Recombinant Proteins
  • Eugenol
  • Hydroxyacetylaminofluorene
  • Guaiacol
  • Arylsulfotransferase

Associated data

  • GENBANK/AF033653