Extreme Thermophiles

Author(s):  
Dennis W Grogan
Keyword(s):  
2009 ◽  
Vol 32 (3) ◽  
pp. 177-185 ◽  
Author(s):  
Angel Angelov ◽  
Markus Mientus ◽  
Susanne Liebl ◽  
Wolfgang Liebl

Author(s):  
Juergen Wiegel ◽  
Francesco Canganella
Keyword(s):  

Author(s):  
Roy M. Daniel ◽  
H. W. Morgan ◽  
A. M. Donnison
Keyword(s):  

1979 ◽  
Vol 177 (2) ◽  
pp. 441-448 ◽  
Author(s):  
I P Wright ◽  
T K Sundaram

Malate dehydrogenase from a number of bacteria drawn from several genera and representing the mesophilic, moderately thermophilic and extremely thermophilic classes was isolated by procedures which involve only a small number of steps (in most cases only two), of which the key one is affinity chromatography on 5′-AMP–Sepharose and/or on NAD+–hexane–agarose. Electrophoretic analysis of the native enzymes in polyacrylamide gel and of the denaturated enzymes in sodium dodecyl sulphate/polyacrylamide gel revealed no significant protein impurity in the purified preparations. The yields ranged from about 40% to over 80%. The malate dehydrogenases from the extreme thermophiles and from some of the moderate thermophiles are appreciably less efficient catalytically than their mesophilic homologues.


2005 ◽  
Vol 388 (2) ◽  
pp. 427-433 ◽  
Author(s):  
Yusuke TERUI ◽  
Mio OHNUMA ◽  
Kaori HIRAGA ◽  
Etsuko KAWASHIMA ◽  
Tairo OSHIMA

Extreme thermophiles produce two types of unusual polyamine: long linear polyamines such as caldopentamine and caldohexamine, and branched polyamines such as quaternary ammonium compounds [e.g. tetrakis(3-aminopropyl)ammonium]. To clarify the physiological roles of long linear and branched polyamines in thermophiles, we synthesized them chemically and tested their effects on the stability of ds (double-stranded) and ss (single-stranded) DNAs and tRNA in response to thermal denaturation, as measured by differential scanning calorimetry. Linear polyamines stabilized dsDNA in proportion to the number of amino nitrogen atoms within their molecular structure. We used the empirical results to derive formulae that estimate the melting temperature of dsDNA in the presence of polyamines of a particular molecular composition. ssDNA and tRNA were stabilized more effectively by tetrakis(3-aminopropyl)ammonium than any of the other polyamines tested. We propose that long linear polyamines are effective to stabilize DNA, and tetrakis(3-aminopropyl)ammonium plays important roles in stabilizing RNAs in thermophile cells.


1987 ◽  
Vol 53 (4) ◽  
pp. 832-838 ◽  
Author(s):  
Christopher H. Sissons ◽  
Keith R. Sharrock ◽  
Roy M. Daniel ◽  
Hugh W. Morgan

2012 ◽  
Vol 26 (S1) ◽  
Author(s):  
Jennie E. Williams ◽  
Julie N. Reitter ◽  
Kenneth V. Mills

1995 ◽  
Vol 305 (1) ◽  
pp. 17-20 ◽  
Author(s):  
N More ◽  
R M Daniel ◽  
H H Petach

The stability of two enzymes from extreme thermophiles (glutamate dehydrogenase from Thermococcales strain AN1 and beta-glucosidase from Caldocellum saccharolyticum expressed in Escherichia coli) has been exploited to allow measurement of activity over a 175 degrees C temperature range, from +90 degrees C to -85 degrees C for the glutamate dehydrogenase and from +90 degrees C to -70 degrees C for the beta-glucosidase. The Arrhenius plots of these enzymes, and those for two mesophilic enzymes (glutamate dehydrogenase from bovine liver and beta-galactosidase from Escherichia coli), exhibit no downward deflection corresponding to the glass transition, found by biophysical measurements of several non-enzymic mesophilic proteins at about -65 degrees C and reflecting a sharp decrease in protein flexibility as the overall motion of groups of atoms ceases.


Sign in / Sign up

Export Citation Format

Share Document