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• W1996340902 abstract "The function of an ATP-dependent membrane protease FtsH was investigated using the enzyme from Thermus thermophilus HB8. An FtsH mutant with replacement of Glu-419 in the zinc-binding motif by Cys lost the activity to digest casein, a model unfolded protein, and the small ATPase activity of this mutant was no longer stimulated by casein. In the presence of ATP or ATPgammaS, but not ADP, a mutant FtsH-unfolded protein complex was isolated, indicating that ATP binding, but not ATP hydrolysis, is required for FtsH to form a stable complex with an unfolded protein. The FtsH without mutation at Glu-419 did not produce a stable complex with casein in the presence of any nucleotides tested and therefore it appears that blocking proteolysis also contributes to stabilization of the complex." @default.
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• W1996340902 date "2002-08-01" @default.
• W1996340902 modified "2023-10-16" @default.
• W1996340902 title "Stabilization of FtsH-unfolded protein complex by binding of ATP and blocking of protease" @default.
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• W1996340902 doi "https://doi.org/10.1016/s0006-291x(02)00830-6" @default.
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