Manipulation of the tuf gene provides clues to the localization of sequence element(s) involved in the thermal stability of Thermatoga maritima elongation factor Tu

Article Abstract:

Truncated versions of the tuf gene for elongation factor Tu (EF-Tu) from the hyperthermophilic bacterium Thermotoga maritima, were generated by progressive 3' - 5' trimming. The truncated genes were expressed in Escherichia coli and the thermal stability of the gene products were studied. One of the truncated proteins, corresponding to the nucleotide-binding domain seems to be only slightly less stable than the full-length EF-Tu. Replacement of the first 90 N-terminal residues of both the full-length Thermotoga EF-Tu and the isolated G domain with the corresponding sequence of the mesophilic bacterium E. coli, drastically destabilizes both the complete and the truncated protein, suggesting that sequence element(s) that are crucial to Tu lie well within the initial segment of the G domain between residues 1 and 90.

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Analysis of a Thermotoga maritima DNA fragment encoding two similar thermostable cellulases, CelA and CelB, and characterization of the recombinant enzymes

Article Abstract:

Recombinant Escherichia coli clones exhibiting thermostable beta-glucanase activity were isolated from two different gene libraries of the hyperthermophilic bacterium Thermotoga maritima MSB8 (DSM 3109), and the nucleotide sequence of a 1,4,-beta-glucanase gene called celA was determined. CelA had a molecular mass of 29.732 kDa and was most active against soluble substrates. CelA also exhibited astonishing thermostability, which was heightened by the presence of high concentrations of salt.

Genetic aspects, Nucleotide sequence, Base sequence

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Characterization of glycolipids from Meiothermus spp

Article Abstract:

A study was conducted to analyze the characterization of the glycolipids from the type strains of Meiothermus ruber, Meiothermus chliarophilus, Meiothermus silvanus and Meiothermus cerbereus. Fast atom bombardment and chemical techniques were utilized to carry out the analysis. Results indicated that the presence of glycolipids supporting 2-hydroxyacyl groups N-linked to hexosamine is a stable phenotypic marker that distinguishes the genus Meiothermus from the genus Thermus.

Glycolipids

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