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Appl Environ Microbiol, March 1998, p. 896-901, Vol. 64, No. 3
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Transcription of ppk from Acinetobacter sp. Strain ADP1, Encoding a Putative Polyphosphate Kinase, Is Induced by Phosphate Starvation

Walter Geißdörfer, Andreas Ratajczak, and Wolfgang Hillen*

Lehrstuhl für Mikrobiologie, Institut für Mikrobiologie, Biochemie und Genetik der Friedrich-Alexander-Universität Erlangen-Nürnberg, 91058 Erlangen, Germany

Received 30 September 1997/Accepted 9 December 1997

Polyphosphate kinase (Ppk) catalyzes the formation of polyphosphate from ATP. We cloned the ppk gene (2,073 bp) from Acinetobacter sp. strain ADP1; this gene encodes a putative polypeptide of 78.6 kDa with extensive homology to polyphosphate kinase from Escherichia coli and other bacteria. Chromosomal disruption of ppk by inserting a transcriptionally fused lacZ does not affect growth under conditions of phosphate limitation or excess. beta -Galactosidase activity expressed from the single-copy ppk::lacZ fusion is induced 5- to 15-fold by phosphate starvation. An increased amount of ppk transcript (2.2 kb) was detected when cells were grown at a limiting phosphate concentration. Primer extension analysis revealed a regulated promoter located upstream of a second, constitutive promoter. Potential similarities of this regulation with the effects of PhoB and PhoR of E. coli are discussed.

* Corresponding author. Mailing address: Lehrstuhl für Mikrobiologie, Institut für Mikrobiologie, Biochemie und Genetik der Friedrich-Alexander-Universität Erlangen-Nürnberg, Staudtstrasse 5, 91058 Erlangen, Germany. Phone: 49 (9131) 858081. Fax: 49 (9131) 858082. E-mail: whillen{at}biologie.uni-erlangen.de.




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Copyright © 1998 by the American Society for Microbiology. All rights reserved.