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Journal of Bacteriology, July 2000, p. 3681-3687, Vol. 182, No. 13
Department of
Biochemistry1 and Department of
Bacteriology,2 University of
Wisconsin-Madison, Madison, Wisconsin 53706
Received 12 January 2000/Accepted 4 April 2000
The redox state of nitrogenase Fe protein is shown to affect
regulation of ADP-ribosylation in Klebsiella pneumoniae
strains transformed by plasmids carrying dra genes from
Rhodospirillum rubrum. The dra operon encodes
dinitrogenase reductase ADP-ribosyltransferase and dinitrogenase
reductase-activating glycohydrolase, enzymes responsible for the
reversible inactivation, via ADP-ribosylation, of nitrogenase Fe
protein in R. rubrum. In bacteria containing the
dra operon in their chromosomes, inactivation occurs in
response to energy limitation or nitrogen sufficiency. The
dra gene products, expressed at a low level in K. pneumoniae, enable transformants to reversibly
ADP-ribosylate nitrogenase Fe protein in response to the presence of
fixed nitrogen. The activities of both regulatory enzymes are regulated
in vivo as described in R. rubrum. Genetic perturbations of
the nitrogenase electron transport chain were found to affect the rate
of inactivation of Fe protein. Strains lacking the electron donors to
Fe protein (NifF or NifJ) were found to inactivate Fe protein more
quickly than a strain with wild-type background. Deletion of
nifD, which encodes a subunit of nitrogenase MoFe protein,
was found to result in a slower inactivation response. No variation was
found in the reactivation responses of these strains. It is concluded
that the redox state of the Fe protein contributes to the regulation of
the ADP-ribosylation of Fe protein.
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Effects of Perturbations of the Nitrogenase Electron Transfer
Chain on Reversible ADP-Ribosylation of Nitrogenase Fe Protein
in Klebsiella pneumoniae Strains Bearing the
Rhodospirillum rubrum dra Operon
*
Corresponding author. Mailing address: Department of
Biochemistry, University of Wisconsin-Madison, Madison, WI 53706. Phone: (608) 262-6859. Fax: (608) 262-3453. E-mail:
ludden{at}biochem.wisc.edu.
Journal of Bacteriology, July 2000, p. 3681-3687, Vol. 182, No. 13
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
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