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Journal of Bacteriology, August 2004, p. 5418-5426, Vol. 186, No. 16
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.16.5418-5426.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Differential Regulation of Soluble and Membrane-Bound Inorganic Pyrophosphatases in the Photosynthetic Bacterium Rhodospirillum rubrum Provides Insights into Pyrophosphate-Based Stress Bioenergetics

Rosa L. López-Marqués, José R. Pérez-Castiñeira, Manuel Losada, and Aurelio Serrano*

Instituto de Bioquímica Vegetal y Fotosíntesis, Universidad de Sevilla-CSIC, 41092 Seville, Spain

Received 4 February 2004/ Accepted 14 May 2004

Soluble and membrane-bound inorganic pyrophosphatases (sPPase and H+-PPase, respectively) of the purple nonsulfur bacterium Rhodospirillum rubrum are differentially regulated by environmental growth conditions. Both proteins and their transcripts were found in cells of anaerobic phototrophic batch cultures along all growth phases, although they displayed different time patterns. However, in aerobic cells that grow in the dark, which exhibited the highest growth rates, Northern and Western blot analyses as well as activity assays demonstrated high sPPase levels but no H+-PPase. It is noteworthy that H+-PPase is highly expressed in aerobic cells under acute salt stress (1 M NaCl). H+-PPase was also present in anaerobic cells growing at reduced rates in the dark under either fermentative or anaerobic respiratory conditions. Since H+-PPase was detected not only under all anaerobic growth conditions but also under salt stress in aerobiosis, the corresponding gene is not invariably repressed by oxygen. Primer extension analyses showed that, under all anaerobic conditions tested, the R. rubrum H+-PPase gene utilizes two activator-dependent tandem promoters, one with an FNR-like sequence motif and the other with a RegA motif, whereas in aerobiosis under salt stress, the H+-PPase gene is transcribed from two further tandem promoters involving other transcription factors. These results demonstrate a tight transcriptional regulation of the H+-PPase gene, which appears to be induced in response to a variety of environmental conditions, all of which constrain cell energetics.


* Corresponding author. Mailing address: Instituto de Bioquímica Vegetal y Fotosíntesis, Universidad de Sevilla-CSIC, Avda. Américo Vespucio, s/n, 41092 Seville, Spain. Phone: 34-95-4489524. Fax: 34-95-4460065. E-mail: aurelio{at}cica.es.


Journal of Bacteriology, August 2004, p. 5418-5426, Vol. 186, No. 16
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.16.5418-5426.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Au, K. M., Barabote, R. D., Hu, K. Y., Saier, M. H. Jr (2006). Evolutionary appearance of H+-translocating pyrophosphatases.. Microbiology 152: 1243-1247 [Full Text]  
  • Seufferheld, M., Lea, C. R., Vieira, M., Oldfield, E., Docampo, R. (2004). The H+-pyrophosphatase of Rhodospirillum rubrum Is Predominantly Located in Polyphosphate-rich Acidocalcisomes. J. Biol. Chem. 279: 51193-51202 [Abstract] [Full Text]