| First Author | Ouyang YB | Year | 1998 |
| Journal | J Biol Chem | Volume | 273 |
| Issue | 38 | Pages | 24770-4 |
| PubMed ID | 9733778 | Mgi Jnum | J:50099 |
| Mgi Id | MGI:1289861 | Doi | 10.1074/jbc.273.38.24770 |
| Citation | Ouyang YB, et al. (1998) Molecular cloning and expression of human and mouse tyrosylprotein sulfotransferase-2 and a tyrosylprotein sulfotransferase homologue in Caenorhabditis elegans. J Biol Chem 273(38):24770-4 |
| abstractText | Tyrosine O-sulfation, a common post-translational modification in eukaryotes, is mediated by Gels enzymes that catalyze the transfer of the sulfuryl group from 3'- phosphoadenosine 5'-phosphosulfate to tyrosine residues in polypeptides. We recently isolated cDNAs encoding human and mouse tyrosylprotein sulfotransferase-l (Ouyang, Y. B., Lane, W. S., and Moore, K. L. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 2896-2901). Here we report the isolation of cDNAs encoding a second tyrosylprotein sulfotransferase (TPST), designated TPST-2. The human and mouse TPST-2 cDNAs predict type II transmembrane proteins of 377 and 376 amino acid residues, respectively. The cDNAs encode functional N-glycosylated enzymes when expressed in mammalian cells. In addition, preliminary analysis indicates that TPST-1 and TPST-2 have distinct specificities toward peptide substrates. The human TPST-2 gene is on chromosome 22q12.1, and the mouse gene is in the central region of chromosome 5. We have also identified a cDNA that encodes a TPST in the nematode Caenorhabditis elegans that maps to the right arm of chromosome III. Thus, we have identified two new members of a class of membrane-bound sulfotransferases that catalyze tyrosine O-sulfation. These enzymes may catalyze tyrosine O-sulfation of a variety of protein substrates involved in diverse physiologic functions. |
