Journal of Bacteriology, July 1999, p. 4430-4434, Vol. 181, No. 14
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Section of Microbiology, Division of Biological Sciences, University of California, Davis, California 95616
Received 23 February 1999/Accepted 11 May 1999
In a test of the hypothesis that DevR is a response regulator
protein that functions in a phosphorelay signal transduction system
involved in heterocyst development in Nostoc punctiforme ATCC 29133, purified affinity-tagged DevR was shown to be
phosphorylated in vitro by the noncognate sensor kinase EnvZ.
Site-directed mutagenesis was used to generate N. punctiforme mutants with single amino acid substitutions at the
putative phosphorylation site of DevR. These mutants exhibited a
Fox
phenotype like the original devR
insertion mutant UCD 311, consistent with a phosphotransferase role for DevR.
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