The N-terminal sequence after residue 247 plays an important role in structure and function of Lon protease from Brevibacillus thermoruber WR-249 |
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Authors: | Jiun-Ly Chir Yu-Ching Lin |
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Institution: | a Institute of Biological Chemistry, Academia Sinica, 128 Academia Road, Sec. 2, Nankang, Taipei 115, Taiwan b Institute of Biochemical Sciences, National Taiwan University, Taipei 106, Taiwan |
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Abstract: | Previous studies on the N-terminal domain of Lon proteases have not clearly identified its function. Here we constructed randomly chosen N-terminal-truncated mutants of the Lon protease from Brevibacillus thermoruber WR-249 to elucidate the structure-function relationship of this domain. Mutants lacking amino acids from 1 to 247 of N terminus retained significant peptidase and ATPase activities, but lost ∼90% of protease activity. Further truncation of the protein resulted in the loss of all three activities. Mutants lacking amino acids 246-259 or 248-256 also lost all activities and quaternary structure. Our results indicated that amino acids 248-256 (SEVDELRAQ) are important for the full function of the Lon protease. |
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Keywords: | Lon protease ATP-dependent protease Gel filtration chromatography Brevibacillus thermoruber |
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