This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Geißdörfer, W.
Right arrow Articles by Hillen, W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Geißdörfer, W.
Right arrow Articles by Hillen, W.
Agricola
Right arrow Articles by Geißdörfer, W.
Right arrow Articles by Hillen, W.

 Previous Article  |  Next Article 

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.




This article has been cited by other articles:

  • Ghorbel, S., Smirnov, A., Chouayekh, H., Sperandio, B., Esnault, C., Kormanec, J., Virolle, M.-J. (2006). Regulation of ppk Expression and In Vivo Function of Ppk in Streptomyces lividans TK24.. J. Bacteriol. 188: 6269-6276 [Abstract] [Full Text]  
  • Elbahloul, Y., Steinbuchel, A. (2006). Engineering the Genotype of Acinetobacter sp. Strain ADP1 To Enhance Biosynthesis of Cyanophycin. Appl. Environ. Microbiol. 72: 1410-1419 [Abstract] [Full Text]  
  • Ishige, T., Krause, M., Bott, M., Wendisch, V. F., Sahm, H. (2003). The Phosphate Starvation Stimulon of Corynebacterium glutamicum Determined by DNA Microarray Analyses. J. Bacteriol. 185: 4519-4529 [Abstract] [Full Text]  
  • Chen, W., Palmer, R. J., Kuramitsu, H. K. (2002). Role of Polyphosphate Kinase in Biofilm Formation by Porphyromonas gingivalis. Infect. Immun. 70: 4708-4715 [Abstract] [Full Text]  
  • Ogawa, N., Tzeng, C.-M., Fraley, C. D., Kornberg, A. (2000). Inorganic Polyphosphate in Vibrio cholerae: Genetic, Biochemical, and Physiologic Features. J. Bacteriol. 182: 6687-6693 [Abstract] [Full Text]  
  • McGrath, J. W., Quinn, J. P. (2000). Intracellular Accumulation of Polyphosphate by the Yeast Candida humicola G-1 in Response to Acid pH. Appl. Environ. Microbiol. 66: 4068-4073 [Abstract] [Full Text]  
  • Tzeng, C.-M., Kornberg, A. (2000). The Multiple Activities of Polyphosphate Kinase of Escherichia coli and Their Subunit Structure Determined by Radiation Target Analysis. J. Biol. Chem. 275: 3977-3983 [Abstract] [Full Text]  
  • Gavigan, J.-A., Marshall, L. M., Dobson, A. D. W. (1999). Regulation of polyphosphate kinase gene expression in Acinetobacter baumannii 252. Microbiology 145: 2931-2937 [Abstract] [Full Text]  
  • Trelstad, P. L., Purdhani, P., Geißdörfer, W., Hillen, W., Keasling, J. D. (1999). Polyphosphate Kinase of Acinetobacter sp. Strain ADP1: Purification and Characterization of the Enzyme and Its Role during Changes in Extracellular Phosphate Levels. Appl. Environ. Microbiol. 65: 3780-3786 [Abstract] [Full Text]  
  • Geißdörfer, W., Kok, R. G., Ratajczak, A., Hellingwerf, K. J., Hillen, W. (1999). The Genes rubA and rubB for Alkane Degradation in Acinetobacter sp. Strain ADP1 Are in an Operon with estB, Encoding an Esterase, and oxyR. J. Bacteriol. 181: 4292-4298 [Abstract] [Full Text]  
  • Zago, A., Chugani, S., Chakrabarty, A. M. (1999). Cloning and Characterization of Polyphosphate Kinase and Exopolyphosphatase Genes from Pseudomonas aeruginosa 8830. Appl. Environ. Microbiol. 65: 2065-2071 [Abstract] [Full Text]  
  • Ratajczak, A., Geißdörfer, W., Hillen, W. (1998). Expression of Alkane Hydroxylase from Acinetobacter sp. Strain ADP1 Is Induced by a Broad Range of n-Alkanes and Requires the Transcriptional Activator AlkR. J. Bacteriol. 180: 5822-5827 [Abstract] [Full Text]  
  • Ratajczak, A., Geißdörfer, W., Hillen, W. (1998). Alkane Hydroxylase from Acinetobacter sp. Strain ADP1 Is Encoded by alkM and Belongs to a New Family of Bacterial Integral-Membrane Hydrocarbon Hydroxylases. Appl. Environ. Microbiol. 64: 1175-1179 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»