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(Received for publication, October 15, 1996, and in revised form, November 12, 1996)
From the Department of Applied Biological Sciences, School of
Agricultural Sciences, Nagoya University, Nagoya 464-01, Japan
Of the four genes (nrtABCD) required
for active transport of nitrate in the cyanobacterium
Synechococcus sp. strain PCC 7942, nrtBCD
encode membrane components of an ATP-binding cassette transporter involved in the transport of nitrite as well as of nitrate, whereas nrtA encodes a 45-kDa cytoplasmic membrane protein, the
biochemical function of which remains unclear. Characterization of the
nrtA deletional mutants showed that the 45-kDa protein is
essential for the functioning of the nitrate/nitrite transporter. A
truncated NrtA protein lacking the N-terminal 81 amino acids, expressed in Escherichia coli cells as a histidine-tagged soluble
protein, was shown to bind nitrate and nitrite with high affinity
(Kd = 0.3 µM). Immunoblotting
analysis using the antibody against the 45-kDa protein revealed a
48-kDa precursor of the protein, which accumulated in the
cyanobacterial cells treated with globomycin, an antibiotic that
specifically inhibits cleavage of the signal peptide of lipoprotein
precursors. These findings indicated that the nrtA gene
product is a nitrate- and nitrite-binding lipoprotein. The N-terminal
sequences of putative cyanobacterial substrate-binding proteins
suggested that lipoprotein modification of substrate-binding proteins
of ATP-binding cassette transporters is common in cyanobacteria.
Volume 272, Number 5,
Issue of January 31, 1997
pp. 3036-3041
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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