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(Received for publication, February 24, 1995; and in revised form, April
10, 1995) The precursor of the chloroplast flavoprotein
ferredoxin-NADP
Volume 270,
Number 34,
Issue of August 25, pp. 19930-19935, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Reductase Synthesized
in Escherichia coli Contains Bound FAD and Is Transported into
Chloroplasts
reductase from pea was expressed in Escherichia coli as a carboxyl-terminal fusion to glutathione S-transferase. The fused protein was soluble, and the
precursor could be purified in a few steps involving affinity
chromatography on glutathione-agarose, cleavage of the transferase
portion by protease Xa, and ion exchange chromatography on
DEAE-cellulose. The purified prereductase contained bound FAD but
displayed marginally low levels of activity. Removal of the transit
peptide by limited proteolysis rendered a functional protease-resistant
core exhibiting enzymatic activity. The FAD-containing precursor
expressed in E. coli was readily transported into isolated pea
chloroplasts and was processed to the mature size, both inside the
plastid and by incubation with stromal extracts in a plastid-free
reaction. Import was dependent on the presence of ATP and was
stimulated severalfold by the addition of plant leaf extracts.
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