Journal of Biochemistry 2009-09-01

Molecular cloning, expression and characterization of a novel mouse SULT6 cytosolic sulfotransferase.

Saki Takahashi, Yoichi Sakakibara, Emi Mishiro, Haruna Kouriki, Rika Nobe, Katsuhisa Kurogi, Shin Yasuda, Ming-Cheh Liu, Masahito Suiko

Index: J. Biochem. 146(3) , 399-405, (2009)

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Abstract

By searching the mouse EST database, we identified a novel mouse cytosolic sulfotransferase (SULT) cDNA (RIKEN cDNA 2410078J06). Sequence analysis revealed that this new SULT belongs to the cytosolic SULT6 gene family. The recombinant form of this newly identified SULT, designated SULT6B1, was expressed using the pGEX-4T-1 glutathione S-transferase fusion system and purified from transformed BL21 Escherichia coli cells. Purified mouse SULT6B1 exhibited sulfonating activity toward thyroxine and bithionol among a variety of endogenous and xenobiotic compounds tested as substrates. pH optimum of purified mouse SULT6B1 was determined to be 8.0. Tissue-specific expression of mouse and human SULT6B1 was examined by RT-PCR. While human SULT6B1 was specifically expressed in kidney and testis, mouse SULT6B1 was detected in brain, heart, kidney, thymus, lung, liver and testis. Further studies are needed in order to clarify the role of SULT6B1 in the metabolism of thyroxine and possibly some xenobiotics in mouse.