Polypeptide elongation factor Tu from Halobacterium marismortui.
A GDP-binding protein of 60 kDa from Halobacterium marismortui has been purified to homogeneity. The purification has been carried out in high-salt buffers or in 50% glycerol buffers to protect the halophilic protein from denaturation. Evidence that this protein is the halophilic elongation factor Tu (hEF-Tu) is provided by the high homology of its N terminus with the corresponding sequences of other EF-Tus, and by immunological studies. Like some other EF-Tus the native protein can be cleaved with trypsin without concomitant loss of GDP-binding ability. The molecular mass of this hEF-Tu is higher than that for the corresponding factors from other sources including the halobacterium Halobacterium cutirubrum. The protein possesses typical halophilic characteristics, in that it is stable and active in 3 M KCl or 2 M (NH4)2SO4. Some other properties, like autofragmentation under sample treatment before SDS-PAGE, are described.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000302:isolation & purification; D004591:Electrophoresis, Polyacrylamide Gel; D019204:GTP-Binding Proteins / Q000302:isolation & purification; D006217:Halobacterium / Q000032:analysis*; D010444:Peptide Elongation Factor Tu / Q000276:immunology / Q000302:isolation & purification*; D011489:Protein Denaturation
D000596:Amino Acids; D019204:GTP-Binding Proteins; D010444:Peptide Elongation Factor Tu