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Plant Physiol, July 2000, Vol. 123, pp. 1087-1096
Characterization of Sulfate Assimilation in Marine Algae Focusing
on the Enzyme 5'-Adenylylsulfate Reductase1
Yu
Gao,*
Oscar M.E.
Schofield, and
Thomas
Leustek
Biotechnology Center for Agriculture and the Environment and
Institute of Marine and Coastal Sciences, Rutgers University, New
Brunswick, New Jersey 08901-8520
5'-Adenylylsulfate (APS) reductase was characterized in diverse
marine algae. A cDNA encoding APS reductase from Enteromorpha intestinalis (EAPR) was cloned by functional complementation of an Escherichia coli cysH mutant. The deduced amino acid
sequence shows high homology with APS reductase (APR) from flowering
plants. Based on the probable transit peptide cleavage site the mature protein is 45.7 kD. EAPR expressed as a His-tagged recombinant protein catalyzes reduced glutathione-dependent reduction of APS to
sulfite, exhibiting a specific activity of approximately 40 µmol
min 1 mg protein1 and Michealis-Menten
kinetic constants of approximately 1.4 mM for reduced
glutathione and approximately 6.5 µM for APS. APR activity and expression were studied in relation to the production of
3-dimethylsulfoniopropionate (DMSP), a sulfonium compound produced by
many marine algae. A diverse group of DMSP-producing species showed
extremely high enzyme activity (up to 400 times that found in flowering
plants). Antibodies raised against a conserved peptide of APR strongly
cross-reacted with a protein of 45 kD in several chlorophytes but
insignificantly with chromophytes. In the chlorophyte Tetraselmis sp., APR activity varies significantly
during the culture cycle and does not follow the changes in cellular
DMSP content. However, a positive correlation was found between
cell-based APR activity and specific growth rate.
1
This work was supported by the National Science
Foundation (grant nos. IBN-9601146 and IBN-9817594), the Office of
Naval Research (grant no. N00014-96-0212 to T.L.), and the
Agricultural Research Service cooperative agreement (grant no.
58-6435-6-028 to O.M.E.S.).
*
Corresponding author; e-mail gao{at}aesop.rutgers.edu; fax
732-932-0312.
© 2000 American Society of Plant Physiologists
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