Molecular Cloning, Expression and Characterization of A Novel Mouse SULT6 Cytosolic Sulfotransferase

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 expre...

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Bibliographic Details
Published in:Journal of biochemistry (Tokyo) 2009-09, Vol.146 (3), p.399-405
Main Authors: Takahashi, Saki, Sakakibara, Yoichi, Mishiro, Emi, Kouriki, Haruna, Nobe, Rika, Kurogi, Katsuhisa, Yasuda, Shin, Liu, Ming-Cheh, Suiko, Masahito
Format: Article
Language:English
Subjects:
Amino Acid Motifs
Amino Acid Sequence
Animals
Bithionol - metabolism
Cloning, Molecular
detoxification
DNA, Complementary - metabolism
Expressed Sequence Tags
Female
Gene Expression
Gene Library
Humans
Hydrogen-Ion Concentration
Kinetics
Male
metabolism
Mice
Molecular Sequence Data
Myocardium - enzymology
Organ Specificity
Phosphoadenosine Phosphosulfate - metabolism
Phylogeny
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - isolation & purification
Recombinant Fusion Proteins - metabolism
Reverse Transcriptase Polymerase Chain Reaction
Sequence Alignment
Sequence Homology, Amino Acid
Substrate Specificity
sulfonation
sulfotransferase
Sulfotransferases - chemistry
Sulfotransferases - genetics
Sulfotransferases - metabolism
thyroxine
Thyroxine - metabolism
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Summary: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.
ISSN:0021-924X
1756-2651
DOI:10.1093/jb/mvp087