APS‐sulfotransferase activity is identical to higher plant APS‐kinase (EC 2.7.1.25)

FEBS Letters

Schwenn, Jens D.¹  Schiffmann, Sandra¹ 

[1] Biochemistry of Plants, Ruhr University Bochum, 44780 Bochum, Germany

关键词: APS-kinase;    APS-sulfotransferase activity;    Gene expression;    Recombinant enzyme;    Arabidopsis thaliana;    APS;    adenosine 5′-phosphosulfate;    bp;    base pair(s);    DTT;    dithiothreitol;    ELISA;    enzyme-linked immunosorbant assay;    HRP;    horseraddish peroxidase;    IPTG;    isopropyl-β-d-thiogalacto-pyranoside;    PAP;    3′-phosphoadenosine 5′-phosphate;    PAPS;    3′-phosphoadenosine 5′-phosphosulfate;    PCR;    polymerase chain reaction;   

DOI  :  10.1016/0014-5793(94)01193-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A cDNA from Arabidopsis thaliana L. Heynh encoding the APS-kinase (EC 2.7.1.25) was modified by deletion of a plastidic transit peptide to enable its expression in Escherichia coli. The resultant protein (MW 25,761) is enzymatically active as APS-kinase and restores prototrophic growth in an APS-kinase mutant. All transformants harbouring the modified plant DNA also acquired APS-sulfotransferase activity. In the absence of ATP but provided with DTT, a tetrameric form of recombinant APS-kinase exhibits APS-sulfotransferase activity. Monospecific polyclonal antibodies raised against the APS-kinase as immunogen also reacted against APS-sulfotransferase. We propose that APS-sulfotransferase activity is a non-physiological side reaction of APS-kinase.

【 授权许可】

Unknown