S alinibacter , the Red Bacterial Extreme Halophile

Author(s):  
Aharon Oren
Keyword(s):  
2009 ◽  
Vol 5 (4) ◽  
pp. e1000332 ◽  
Author(s):  
Orland Gonzalez ◽  
Susanne Gronau ◽  
Friedhelm Pfeiffer ◽  
Eduardo Mendoza ◽  
Ralf Zimmer ◽  
...  

1984 ◽  
Vol 62 (1) ◽  
pp. 44-48 ◽  
Author(s):  
A. T. Gudkov ◽  
S. Yu Venyaminov ◽  
A. T. Matheson

Physical studies on the effect of temperature and ionic conditions on the secondary, tertiary, and quaternary structure of the ribosomal "A" protein, equivalent to L7/L12 in Escherichia coli, from two archaebacteria were performed using circular dichroism and sedimentation equilibrium measurements. The two archaebacteria investigated were Halobacterium cutirubrum, an extreme halophile, and Methanobacterium thermoautotrophicum, a thermophile which also showed properties of a moderate halophile. The changes in the secondary structure and the thermostability of these proteins were directly related to the internal salt concentrations of the two archaebacteria. At the higher salt concentrations the changes in the secondary structure resulted in changes in the tertiary and quaternary structure of these proteins.


RNA ◽  
2003 ◽  
Vol 9 (7) ◽  
pp. 794-801 ◽  
Author(s):  
C. EVILIA
Keyword(s):  

1975 ◽  
Vol 140 (1) ◽  
pp. 15-27 ◽  
Author(s):  
Arne Reider Strøm ◽  
George Oda ◽  
Sadiq Hasnain ◽  
Makoto Yaguchi ◽  
Louis Peter Visentin

1972 ◽  
Vol 18 (7) ◽  
pp. 993-995 ◽  
Author(s):  
Janos K. Lanyi ◽  
Melvin P. Silverman

Intracellular K+ in lysed freeze-thawed cell pastes of the extreme halophile, H. cutirubrum, diffused readily against a concentration gradient during equilibrium dialysis, whereas the intracellular Mg2+ was not readily diffusible. The K+ activity in the lysed cell pastes, determined directly by K+ ion-specific electrode, was comparable to the total K-content of the cells, as determined by atomic absorption. This finding and the results of the dialysis experiment suggest that the intracellular K+ in H. cutirubrum is not bound.


1971 ◽  
Vol 121 (4) ◽  
pp. 621-627 ◽  
Author(s):  
B. Gregory Louis ◽  
P. S. Fitt

1. DNA-dependent RNA polymerase was purified 150-fold from crude extracts of the extreme halophile Halobacterium cutirubrum. 2. The enzyme requires the presence of native DNA and all four nucleoside triphosphates to incorporate 14C-labelled nucleoside triphosphate into an acid-insoluble ribonuclease-sensitive product. 3. It has an absolute requirement for both Mn2+ and Mg2+. 4. The polymerase requires a high salt concentration for stability, but is markedly inhibited by univalent cations. 5. Its molecular weight is very low compared with that of Escherichia coli RNA polymerase.


1983 ◽  
Vol 4 (3) ◽  
pp. 369-381 ◽  
Author(s):  
F. Rodriguez-Valera ◽  
Guadalupe Juez ◽  
D.J. Kushner
Keyword(s):  

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