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 B2, and leukotriene E4. These results mark the first discovery of the sulfation of eicosanoids catalyzed by a distinct sulfotransferase. Copyright 1999 Academic Press.