Aminoacylation in Sulfolobus acidocaldarius and in methanogenic and halophilic archaebacteria |
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Authors: | Reinhard Rauhut Hans-Joachim Gabius Friedrich Cramer |
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Affiliation: | Max - Planck - Institut für Experimentelle Medizin, Abteilung Chemie, Hermann - Rein - Strasse 3, D - 3400, Göttingen, F.R.G. |
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Abstract: | Abstract Phenylalanyl-tRNA synthetase (PRS) from the sulphur-metabolizing thermoacidophilic archaebacterium Sulfolobus acidocaldarius has been purified 150-fold using different chromatographic steps. The enzyme has a M r of 270 000 and exhibits considerable thermostability in a temperature range up to 90°C with optimal activity at 70°C. Conservation of antigenic determinants could not be detected by antibodies against various PRS of all primary kingdoms. As a further means to detect traits of phylogenetic relationship, the cross-species reactivity between PRS and tRNAs of organisms from the three branches of archaebacteria and from all primary kingdoms reveals the group character of all 3 branches of the archaebacterial domain, the sulphur-metabolizing, methanogenic and halophilic archaebacteria. |
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Keywords: | Aminoacyl-tRNA synthetases tRNA-cross-species reactivity evolution thermostability |
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