Journal of Bacteriology, October 1998, p. 5344-5350, Vol. 180, No. 20
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
and
Department of Biochemistry and Molecular
Biology,
Received 29 May 1998/Accepted 11 August 1998
The nitrate and nitrite reductases of Bacillus subtilis
have two different physiological functions. Under conditions of
nitrogen limitation, these enzymes catalyze the reduction of nitrate
via nitrite to ammonia for the anabolic incorporation of nitrogen into
biomolecules. They also function catabolically in anaerobic respiration, which involves the use of nitrate and nitrite as terminal
electron acceptors. Two distinct nitrate reductases, encoded by
narGHI and nasBC, function in anabolic and
catabolic nitrogen metabolism, respectively. However, as reported
herein, a single NADH-dependent, soluble nitrite reductase encoded by the nasDE genes is required for both catabolic and anabolic
processes. The nasDE genes, together with nasBC
(encoding assimilatory nitrate reductase) and nasF
(required for nitrite reductase siroheme cofactor formation),
constitute the nas operon. Data presented show that transcription of nasDEF is driven not only by the
previously characterized nas operon promoter but also from
an internal promoter residing between the nasC and
nasD genes. Transcription from both promoters is activated
by nitrogen limitation during aerobic growth by the nitrogen
regulator, TnrA. However, under conditions of oxygen limitation,
nasDEF expression and nitrite reductase activity were significantly induced. Anaerobic induction of nasDEF
required the ResDE two-component regulatory system and the presence of nitrite, indicating partial coregulation of NasDEF with the respiratory nitrate reductase NarGHI during nitrate respiration.
*
Corresponding author. Present address: Department of
Biochemistry and Molecular Biology, Oregon Graduate Institute of
Science and Technology, P.O. Box 91000, Portland, OR 97291-1000. Phone: (503) 748-1070. Fax: (503) 748-1464. E-mail:
mnakano{at}bmb.ogi.edu.
Present address: Department of Biochemistry and Molecular Biology,
Oregon Graduate Institute of Science and Technology, Portland, OR
97291-1000.
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