cDNA cloning, functional expression, and characterization of chicken sulfotransferases belonging to the SULT1B and SULT1C families.

Abstract:

:A search of the chicken expressed sequence tag (EST) database identified 2 cDNA clones that appeared to represent members of the SULT1B and SULT1C enzyme families. These cDNAs were fully sequenced and found to contain full-length inserts. Phylogenetic analysis of the derived amino acid sequences clearly placed them as the first members of the chicken SULT1B and SULT1C families, respectively, to be identified, and we propose they be named SULT1B1 and SULT1C1. (CHICK)SULT1B1 shares approximately 60% amino acid sequence identity with mammalian SULT1B enzymes, whereas the closest neighbor to (CHICK)SULT1C1 was the ortholog (RAT)SULT1C1, with 68% identity. We cloned these cDNAs into the bacterial expression vectors from the pET series. Transformed Escherichia coli cells strongly expressed the recombinant proteins. Purification of the recombinant enzymes from E. coli was accomplished by a three-step procedure involving ammonium sulfate precipitation, anion exchange chromatography, and affinity chromatography. The purified enzymes displayed subunit molecular weights of approximately 35,000Da on SDS-PAGE, as predicted, and were both able to sulfate a wide range of compounds, including xenobiotics and endogenous substrates such as iodothyronines. Detailed kinetic analysis showed SULT1C1 was more prolific in that it was able to sulfate dopamine, tyramine, and apomorphine, which SULT1B1 was not. 2-Bromophenol was the best substrate for both enzymes. We also raised antibodies against these proteins, which were able to detect the SULTs by ELISA, and which were able to strongly inhibit the recombinant enzymes. This is the first detailed characterization of sulfotransferases from the chicken, and it demonstrates that the avian and mammalian SULT1 enzymes are closely related in both structure and function.

journal_name

Arch Biochem Biophys

authors

Wilson LA,Reyns GE,Darras VM,Coughtrie MW

doi

10.1016/j.abb.2004.05.008

subject

Has Abstract

pub_date

2004-08-01 00:00:00

pages

64-72

issue

1

eissn

0003-9861

issn

1096-0384

pii

S0003986104003029

journal_volume

428

pub_type

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