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Journal of Bacteriology, August 1998, p. 4044-4050, Vol. 180, No. 16
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
A Redox-Responsive Pathway for Aerobic Regulation
of Photosynthesis Gene Expression in Rhodobacter
sphaeroides 2.4.1
James P.
O'Gara,
Jesus M.
Eraso, and
Samuel
Kaplan*
Department of Microbiology and Molecular
Genetics, The University of Texas Medical School, Houston, Texas
77030
Received 3 April 1998/Accepted 4 June 1998
To further understand the proposed signal transduction pathway
involving the presumed redox proteins RdxBH and
cbb3 cytochrome oxidase in Rhodobacter
sphaeroides 2.4.1, a series of mutants lacking components of
both the Prr two-component activation system and the
cbb3-type cytochrome oxidase or RdxBH were
constructed. We report that under highly aerobic conditions, aberrant
photosynthesis gene expression and spectral complex formation typical
of cbb3- or RdxBH-deficient mutants were no
longer observed when either prrA (encoding the response
regulator of the Prr system) or prrB (encoding the presumed
sensor kinase) was also deleted. These double-mutant strains are
phenotypically identical to single-mutant PrrA and PrrB strains,
suggesting that the signal(s) originating from the
cbb3 terminal oxidase affects downstream
puc and puf operon expression by acting
exclusively through the Prr system. When the same double-mutant strains
were examined under anaerobic dark dimethyl sulfoxide growth
conditions, photosynthesis gene expression was obligatorily linked to
the two-component activation system. However, photosynthesis gene
expression under the same growth conditions was significantly higher in
the cbb3 mutant strain when compared to that in
the wild type. Similarly, under anaerobic photosynthetic conditions the
high levels of the oxidized carotenoid, spheroidenone, which accumulate
in cbb3-deficient mutants were nearly restored
to normal in a PrrB
CcoP
double mutant.
This observation, together with previously published results, suggests
that the regulation of the CrtA-catalyzed reaction possesses both
transcriptional and posttranscriptional regulatory effectors. We
propose that the cbb3 cytochrome oxidase, which by definition can interact with external oxygen, serves to control the
activity of the Prr two-component activation system under both aerobic
and anaerobic conditions. Although independent from the
cbb3 oxidase, the RdxBH proteins are also
required for normal functioning of the Prr two-component activation
system and are therefore believed to lie between the
cbb3 oxidase in this oxygen-sensing, redox
signaling pathway and the Prr activation system.
*
Corresponding author. Mailing address: Department of
Microbiology and Molecular Genetics, The University of Texas Medical School, 6431 Fannin St., Houston, TX 77030. Phone: (713) 500-5502. Fax:
(713) 500-5499. E-mail:
skaplan{at}utmmg.med.uth.tmc.edu.

Present address: Department of Microbiology, Moyne Institute of
Preventive Medicine, The University of Dublin, Trinity College,
Dublin
2, Ireland.
Journal of Bacteriology, August 1998, p. 4044-4050, Vol. 180, No. 16
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
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