A cold-active heat-labile t-RNA modification GTPase from a psychrophilic bacterium Pseudomonas syringae (Lz4W) |
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| Authors: | Ashish Kumar Singh Sisinthy Shivaji |
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| Affiliation: | 1. St John''s Institute of Dermatology, Guy''s and St Thomas'' NHS Foundation Trust, London;2. Department of Dermatopathology, St John''s Institute of Dermatology, Guy''s and St Thomas'' NHS Foundation Trust, London;1. Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka 565-0871, Japan;2. Dept. of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523-1870, USA;3. Janelia Farm Research Campus, Howard Hughes Medical Institute, Ashburn, VA 20147, USA;4. Mab Institute Inc., Sapporo, Hokkaido 001-0021, Japan;5. Department of Biological Sciences, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan |
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| Abstract: | ![]()
A cold-active heat-labile t-RNA modification GTPase (TrmE) from psychrophilic bacterium Pseudomonas syringae (Lz4W) has been purified and characterized. The purified TrmE is a 53 kDa protein, has GTPase activity and hydrolyses only the oxy and deoxy forms of GTP but not the other nucleotide triphosphates. The enzyme exhibits optimal activity at 12–18 °C and retains 65% of its optimal activity at 4 °C, indicating that it is a cold-active enzyme. The enzyme is also heat-labile and loses 60% of its activity at 30 °C. This is the first report on the purification and characterization of a TrmE from a psychrophilic bacterium. |
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