scholarly journals Ubiquitous occurrence of agmatine as the major polyamine within extremely halophilic archaebacteria.

1995 ◽  
Vol 41 (2) ◽  
pp. 153-158 ◽  
Author(s):  
KOEI HAMANA ◽  
HIROSHI HAMANA ◽  
TAKASHI ITOH
Keyword(s):  
Halophilic Archaebacteria

scholarly journals Polyamines in halophilic archaebacteria

1985 ◽  
Vol 28 (3) ◽  
pp. 323-327 ◽  
Author(s):  
M. Carteni-Farina ◽  
M. Porcelli ◽  
G. Cacciapuoti ◽  
M. Rosa ◽  
A. Gambacorta ◽  
...  
Keyword(s):  
Halophilic Archaebacteria

Etophysiology of the aerobic halophilic archaebacteria

1986 ◽  
Vol 7 (2-3) ◽  
pp. 202-212 ◽  
Author(s):  
B.J. Tindall ◽  
H.G. Trüper
Keyword(s):  
Halophilic Archaebacteria

Transformation methods for halophilic archaebacteria

1989 ◽  
Vol 35 (1) ◽  
pp. 148-152 ◽  
Author(s):  
Steven W. Cline ◽  
Wan L. Lam ◽  
Robert L. Charlebois ◽  
Leonard C. Schalkwyk ◽  
W. Ford Doolittle
Keyword(s):  
Molecular Weight ◽  
Plasmid Dna ◽  
Genomic Dna ◽  
Halobacterium Halobium ◽  
Dna Transformation ◽  
Dna Transfection ◽  
Phage Dna ◽  
Halophilic Archaebacteria ◽  
Transformation Methods ◽  
Halobacterium Volcanii

We present a practical description of polyethylene glycol mediated spheroplast transformation of Halobacterium halobium and Halobacterium volcanii. This method has been applied to phage DNA transfection, plasmid DNA transformation, and transformation with linear fragments of high molecular weight genomic DNA. Efficient spheroplast regeneration allows uncomplicated recovery of transformed progeny. Transformations can be performed equally well using fresh or frozen cell preparations. These methods should find application in molecular cloning, genetic fine mapping, and strain construction.Key words: archaebacteria, Halobacterium, transformation methods, spheroplast.

scholarly journals Characterization of a Novel Complex from Halophilic Archaebacteria, Which Displays Chaperone-like Activitiesin Vitro

2001 ◽  
Vol 276 (32) ◽  
pp. 29906-29914 ◽  
Author(s):  
Bruno Franzetti ◽  
Guy Schoehn ◽  
Christine Ebel ◽  
Jean Gagnon ◽  
Rob W. H. Ruigrok ◽  
...  
Keyword(s):  
Halophilic Archaebacteria ◽  
Novel Complex

scholarly journals Antitumor drugs inhibit the growth of halophilic archaebacteria

1987 ◽  
Vol 169 (2) ◽  
pp. 231-236 ◽  
Author(s):  
Mouldy SIOUD ◽  
Giuseppe BALDACCI ◽  
Patrick FORTERRE ◽  
Anne-Marie RECONDO
Keyword(s):  
Antitumor Drugs ◽  
Halophilic Archaebacteria

Intracellular salt concentrations of the anaerobic halophilic eubacteria Haloanaerobium praevalens and Halobacteroides halobius

1986 ◽  
Vol 32 (1) ◽  
pp. 4-9 ◽  
Author(s):  
Aharon Oren
Keyword(s):  
Amino Acids ◽  
Salt Lake ◽  
Compatible Solutes ◽  
Chloride Concentration ◽  
Dead Sea ◽  
Intracellular Potassium ◽  
Acidic Amino Acids ◽  
Nacl Concentration ◽  
Halophilic Archaebacteria ◽  
Eukaryotic Organisms

The obligately anaerobic, moderately halophilic eubacteria Haloanaerobium praevalens (isolated from Great Salt Lake, Utah) and Halobacteroides halobius (isolated from the Dead Sea) were found to contain high intracellular potassium concentrations (0.76–2.05 M, not well correlated with the external NaCl concentration), and high intracellular sodium concentrations (0.28–2.6 M, increasing with increasing extracellular NaCl concentration). The sum of intracellular potassium and sodium concentrations approximated the total cation concentration of the medium. Internal chloride concentrations in Haloanaerobium praevalens equalled the external chloride concentration. Organic solutes, such as betaine, glycerol, and different amino acids that have been shown to serve as compatible solutes in other halophilic eubacteria and eukaryotic organisms, were not found in significant concentrations. Analysis of the amino acids in the proteins of the anaerobic halophilic eubacteria showed an excess of acidic amino acids, similar to that reported in halophilic archaebacteria of the genus Halobacterium.

scholarly journals Dihydrolipoamide dehydrogenase from halophilic archaebacteria

1984 ◽  
Vol 218 (3) ◽  
pp. 811-818 ◽  
Author(s):  
M J Danson ◽  
R Eisenthal ◽  
S Hall ◽  
S R Kessell ◽  
D L Williams
Keyword(s):  
Steady State ◽  
Iodoacetic Acid ◽  
Enzymic Activity ◽  
Evolutionary Significance ◽  
Dihydrolipoamide Dehydrogenase ◽  
Kinetic Measurements ◽  
Steady State Kinetic ◽  
Halophilic Archaebacteria ◽  
Eukaryotic Organisms ◽  
State Kinetic

Dihydrolipoamide dehydrogenase has been discovered in the halophilic archaebacteria for the first time. The enzyme from both classical and alkaliphilic halobacteria has been investigated. (1) The enzyme specifically catalysed the stoichiometric oxidation of dihydrolipoamide by NAD+. Enzymic activity was optimal at 2 M-NaCl and was remarkably resistant to thermal denaturation. (2) The relative molecular masses (Mr) of the native enzyme from the various species of halobacteria were determined to be within the range 112000-120000. (3) The enzyme exhibited a hyperbolic dependence of catalytic activity on both dihydrolipoamide and NAD+ concentrations. From these steady-state kinetic measurements the dissociation constant (Ks) of dihydrolipoamide was determined to be 57 (+/- 5) microM. (4) The enzyme was only susceptible to inactivation by iodoacetic acid in the presence of its reducing ligands, dihydrolipoamide or NADH. The rate of inactivation followed a hyperbolic dependence on the concentration of dihydrolipoamide, from which the Ks of this substrate was calculated to be 55 (+/- 7) microM. Together with the steady-state kinetic data, the pattern of inactivations is consistent with the involvement in catalysis of a reversibly reducible disulphide bond, as has been found in dihydrolipoamide dehydrogenase from non-archaebacterial species. In eubacterial and eukaryotic organisms, dihydrolipoamide dehydrogenase functions in the 2-oxo acid dehydrogenase complexes. These multienzyme systems have not been detected in the archaebacteria, and, in the context of this apparent absence, the possible function and evolutionary significance of archaebacterial dihydrolipoamide dehydrogenase are discussed.

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