Bacterial expression, purification, and characterization of a novel mouse sulfotransferase that catalyzes the sulfation of eicosanoids

Analysis of the nucleotide sequence of a recently cloned mouse sulfotransferase cDNA (clone 679153) revealed the presence in its 3'-untranslated sequence of an AT-rich region which contains four ATTTA motifs and an TTATTTAT-like sequence, commonly found among those encoding inflammation-related proteins. The recombinant enzyme expressed in Escherichia coli and purified to near electrophoretic homogeneity displayed strong sulfotransferase activities toward various prostaglandins, thromboxane B-2, and leukotriene E-4. These results mark the first discovery of the sulfation of eicosanoids catalyzed by a distinct sulfotransferase. (C) 1999 Academic Press.