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Journal of Bacteriology, November 2001, p. 6159-6168, Vol. 183, No. 21
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.21.6159-6168.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Functional Characterization of Three GlnB Homologs
in the Photosynthetic Bacterium Rhodospirillum rubrum:
Roles in Sensing Ammonium and Energy Status
Yaoping
Zhang,1,2,3
Edward L.
Pohlmann,1,3
Paul W.
Ludden,2,3 and
Gary
P.
Roberts1,3,*
Departments of
Bacteriology1 and
Biochemistry2 and Center for the
Study of Nitrogen Fixation,3 University of
Wisconsin-Madison, Madison, Wisconsin 53706
Received 26 February 2001/Accepted 2 August 2001
The GlnB (PII) protein, the product of
glnB, has been characterized previously in the
photosynthetic bacterium Rhodospirillum rubrum. Here we
describe identification of two other PII homologs in this
organism, GlnK and GlnJ. Although the sequences of these three homologs
are very similar, the molecules have both distinct and overlapping
functions in the cell. While GlnB is required for activation of NifA
activity in R. rubrum, GlnK and GlnJ do not appear to be
involved in this process. In contrast, either GlnB or GlnJ can serve as
a critical element in regulation of the reversible ADP ribosylation of
dinitrogenase reductase catalyzed by the dinitrogenase reductase
ADP-ribosyl transferase (DRAT)/dinitrogenase reductase-activating
glycohydrolase (DRAG) regulatory system. Similarly, either GlnB or GlnJ
is necessary for normal growth on a variety of minimal and rich media,
and any of the proteins is sufficient for normal posttranslational
regulation of glutamine synthetase. Surprisingly, in their regulation
of the DRAT/DRAG system, GlnB and GlnJ appeared to be responsive not
only to changes in nitrogen status but also to changes in energy
status, revealing a new role for this family of regulators in central
metabolic regulation.
*
Corresponding author. Mailing address: Department of
Bacteriology, University of Wisconsin-Madison, Madison,
WI 53706. Phone: (608) 262-3567. Fax: (608) 262-9865. E-mail:
groberts{at}bact.wisc.edu.
Journal of Bacteriology, November 2001, p. 6159-6168, Vol. 183, No. 21
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.21.6159-6168.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
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