Characterization of the Membrane-Bound Inorganic Pyrophosphatase in Rhodospirillum rubrum

Randahl, Håkan

doi:10.1111/j.1432-1033.1979.tb06287.x

Cited by 31 publications

(21 citation statements)

References 13 publications

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“…25-kDa subunit), with a K m for MgPP i of 20 to 30 M (29), and an H ϩ -PPase (ca. 60 kDa subunit), an integral membrane protein whose K m for MgPP i is in the range of 0.1 to 0.2 mM (47). In contrast to the situation in photosynthetic eukaryotic tissues that lack a cytosolic sPPase (57), PP i generated in bacterial cell anabolism is presumably accessible to both PPases, since a coordinated regulation is needed in order to maintain an adequate \'0fintracellular level of this metabolite (0.5 to 1.0 mM) (32) and a suitable proton gradient across membranes.…”

Section: Discussionmentioning

confidence: 99%

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

et al. 2004

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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.

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Section: Discussionmentioning

confidence: 99%

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

et al. 2004

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“…In agreement with these conclusions, we found that the A. tumefaciens H ϩ -PPase, the sequence of which has Lys and Thr in the positions investigated (31), is K ϩ -insensitive. Only another proteobacterial H ϩ -PPase has been biochemically characterized, the enzyme from R. rubrum (38,42,43). As this enzyme, the H ϩ -PPase from A. tumefaciens, was sensitive to inhibition by aminomethylenediphosphonate, dicyclohexylcarbodiimide, and N-ethylmaleimide and has low sensitivity to the soluble pyrophosphatase inhibitor fluoride (Fig.…”

Section: Identification Of Organelles In Bacteria 29975mentioning

confidence: 99%

Identification of Organelles in Bacteria Similar to Acidocalcisomes of Unicellular Eukaryotes

Seufferheld

Vieira

Ruiz

et al. 2003

Journal of Biological Chemistry

167

141

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Acidocalcisomes are acidic calcium storage compartments described in several unicellular eukaryotes, including trypanosomatid and apicomplexan parasites, algae, and slime molds. In this work, we report that the volutin granules of Agrobacterium tumefaciens possess properties similar to the acidocalcisomes. Transmission electron microscopy revealed that each intracellular granule was surrounded by a membrane. X-ray microanalysis of the volutin granules showed large amounts of phosphorus, magnesium, potassium, and calcium. Calcium in the volutin granules increased when the bacteria were incubated at high extracellular calcium concentration. Immunofluorescence and immunoelectron microscopy, using antisera raised against peptide sequences conserved in the A. tumefaciens proton pyrophosphatase, indicated localization in intracellular vacuoles. Purification of the volutin granules using iodixanol density gradients indicated a preferential localization of the pyrophosphatase activity in addition to high concentrations of phosphate, pyrophosphate, short-and long-chain polyphosphate, but lack of markers of the plasma membrane. The pyrophosphatase activity was potassium-insensitive and inhibited by the pyrophosphate analogs, amynomethylenediphosphonate and imidodiphosphate, by dicyclohexylcarbodiimide, and by the thiol reagent N-ethylmaleimide. Polyphosphate was also localized to the volutin granules by 4,6-diamino-2-phenylindole staining. The organelles were acidic, as demonstrated by staining with LysoSensor blue DND-167, a dye especially used to detect very acidic compartments in cells, and cycloprodigiosin, a compound isolated from a marine bacterium that has been shown to uncouple proton pyrophosphatase activity acting as a chloride/proton symport. The results suggest that acidocalcisomes arose before the prokaryotic and eukaryotic lineages diverged.

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“…A K ϩ transporting function was proposed for K ϩ -dependent H ϩ -PPases (23), but this issue is still a matter of controversy (14,24). Both K ϩ -dependent and K ϩ -independent H ϩ -PPases are inactivated by sulfhydryl modifying reagents (25)(26)(27)(28)(29)(30).…”

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confidence: 99%

H+-Pyrophosphatase of Rhodospirillum rubrum

Belogurov¹,

Turkina²,

Penttinen³

et al. 2002

Journal of Biological Chemistry

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Characterization of the Membrane-Bound Inorganic Pyrophosphatase in Rhodospirillum rubrum

Cited by 31 publications

References 13 publications

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

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

Identification of Organelles in Bacteria Similar to Acidocalcisomes of Unicellular Eukaryotes

H+-Pyrophosphatase of Rhodospirillum rubrum

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