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| A New Research Highlight on the Lon Protease |
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 A research team led by Dr. Chung-I Chang, an Associate Research Fellow at the Institute of Biological Chemistry found the method to crystallize the Lon protease from Meiothermus taiwanensis and determine its crystal structure, showing how that structure allows the protease to interact with magnesium and the energy molecules ATP and ADP. The research results have been presented in two papers and published back to back in the May issue of Structure; the works have also been featured on Cell’s CrossTalk Blog. (http://crosstalk.cell.com/blog/lon-planet-from-the-taipei-basin-to-nanomachines)
It has been difficult to obtain the 3D structure of an intact Lon protease complex, which is required for protein quality control in both prokaryotes and eukaryotes. It is known that researching “extreme” organisms from hot springs may help answer fundamental biological questions. Dr. Chung-I Chang’s research team took advantage of the rich natural resources of Taiwan, which is full of the resource of hot spring, and investigated the energy-dependent proteolytic machine from the Taiwanese microbe Meiothermus taiwanensis, which can survive the high temperatures of the Wu-Rai hot springs. Dr. Chang’s team developed an important way to crystallize the intact Lon protease complex from Meiothermus taiwanensis and determined its crystal structure. Their discovery underscores the power of using native, local resources to answer global questions.
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