FEBS Letters | |
Thermostable valyl‐tRNA, isoleucyl‐tRNA and methionyl‐tRNA synthetases from an extreme thermophile Thermus thermophilus HB8: protein structure and Zn2+ binding | |
Kohda, Daisuke1  Miyazawa, Tatsuo1  Yokoyama, Shigeyuki1  | |
[1] Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo, Bunkyo-ku, Tokyo 113, Japan | |
关键词: Valyl-tRNA synthetase; Isoleucyl-tRNA synthetase; Methionyl-tRNA synthetase; Thermus thermophilus; Amino acid composition; Zinc content; | |
DOI : 10.1016/0014-5793(84)81069-8 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Thermostable valyl-tRNA, isoleucyl-tRNA and methionyl-tRNA synthetases have been purified from an extreme thermophile, Thermus thermophilus HB8. Valyl-tRNA and isoleucyl-tRNA synthetases are found to be monomer proteins (M r 108000 and 129000, respectively), while methionyl-tRNA synthetase is a dimer protein (M r 150000). These enzymes are very similar with respect to amino acid compositions and α-helix contents as estimated by circular dichroism analyses. Furthermore, two Zn2+ are tightly bound to each of these synthetases. These data suggest that valyl-tRNA and isoleucyl-tRNA synthetases consist of two domains, each corresponding to the subunit of methionyl-tRNA synthetase.
【 授权许可】
Unknown
【 预 览 】
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RO201912020285763ZK.pdf | 312KB | download |