Effect of temperature on stability and activity of elongation factor 2 proteins from Antarctic and thermophilic methanogens.

ABSTRACT: Despite the presence and abundance of archaea in low-temperature environments, little information is available regarding their physiological and biochemical properties. In order to investigate the adaptation of archaeal proteins to low temperatures, we purified and characterized the elongation factor 2 (EF-2) protein from the Antarctic methanogen Methanococcoides burtonii, which was expressed in Escherichia coli, and compared it to the recombinant EF-2 protein from a phylogenetically related thermophile, Methanosarcina thermophila. Using differential scanning calorimetry to assess protein stability and enzyme assays for the intrinsic GTPase activity, we identified biochemical and biophysical properties that are characteristic of the cold-adapted protein. This includes a higher activity at

SUBMITTER: Thomas T 

PROVIDER: S-EPMC94419 | biostudies-literature | 2000 Mar

REPOSITORIES: biostudies-literature