Reconstitution of a Functional Proton-Translocating Adenosine Triphosphatase from the Obligately Anaerobic Bacterium Clostridium pasteurianum

1977 ◽  
Vol 5 (1) ◽  
pp. 140-143 ◽  
Author(s):  
DAVID J. CLARKE ◽  
J. GARETH MORRIS
1976 ◽  
Vol 154 (3) ◽  
pp. 725-729 ◽  
Author(s):  
D J. Clarke ◽  
J. G Morris

The membrane adenosine triphosphatase complex of vegetatively growing Clostridium pasteurianum, solublized with Triton X-100, has been recovered as a significantly purified particulate preparation that is still sensitive to inhibition by dicyclohexylcarbodiimide and butyricin 7423.


1989 ◽  
Vol 67 (6) ◽  
pp. 306-310 ◽  
Author(s):  
Morris F. Manolson ◽  
Judith M. Percy ◽  
David K. Apps ◽  
Xiao-Song Xie ◽  
Dennis K. Stone ◽  
...  

The evolution of the endomembrane systems of eukaryotic cells can be examined by exploring the evolutionary origins of the endomembrane H+-ATPases. Recent studies suggest that certain polypeptides are common to all H+ pumps of this type. Tonoplast H+ -ATPase from Beta vulgaris L. was purified and antibodies raised to two of its subunits. Each of these antisera reacted with a polypeptide of the corresponding size in bovine chromaffin granules, bovine clathrincoated vesicles, and yeast vacuolar membranes, suggesting common structural features and a common ancestor for endomembrane H+-ATPases of different organelles and different kingdoms. The antiserum raised against the 57-kDa polypeptide of plant tonoplast H+ -ATPase also reacted with subunit "a" of the H+-ATPase from the obligately anaerobic bacterium Clostridium pasteurianum and to the α subunit of the H+ -ATPase from Escherichia coli. There was no reactivity with chloroplast or mitochondrial ATPases. These results are discussed in relation to recent sequence data which suggest that endomembrane H+-ATPases may be evolutionarily related to the F0F1 ATPases.Key words: H+ -ATPase, evolution, immunology, vacuole, endomembrane.


1992 ◽  
Vol 4 (2) ◽  
pp. 155-162 ◽  
Author(s):  
P.D. Franzmann ◽  
M. Rohde

An obligately anaerobic bacterium that lacked a cell wall was isolated from the hypolimnion of Ace Lake, Antarctica. Cells were very pleomorphic, forming cocci, filaments up to 25 μm in length, and annular shapes. The organism was morphologically very similar to some members of the class Mollicutes which contains two genera of obligately anaerobic bacteria, Anaeroplasma and Asteroleplasma. Like members of the class, the isolate was resistant to high concentrations of penicillin (1000 Units ml-1). Similar to Anaeroplasma, the organism had a low DNA G+C content (29.3±0.4) and produced hydrogen, carbon dioxide, acetic acid, lactic acid and succinic acid from the fermentation of glucose. However, the taxonomic status of the strain remained unclear as, unlike members of the class Mollicutes, the isolate had a relatively large genome size (2.26±0.11 × 109 daltons), did not pass through 0.45 μm pore size filters, and did not form typical mycoplasma-like colonies. The organism was psychrophilic with an optimum temperature for growth between 12°C and 13°C. A phenotypic description of the organism is given and the ecological role of the organism is inferred from its phenotype and the characteristics of its Antarctic habitat.


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