AAA proteases with catalytic sites on opposite membrane surfaces comprise a proteolytic system for the ATP-dependent degradation of inner membrane proteins in mitochondria.
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Cites background from "AAA proteases with catalytic sites ..."
...Leonhard et al. (1996) suggested that the mitochondrial FtsH-like m-AAA protease participates in the partitioning of a membrane-bound model substrate to the catalytic site by virtue of its chaperone activity, thereby allowing cleavage between residues that normally are embedded in the lipid bilayer....
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Cites background from "AAA proteases with catalytic sites ..."
...Thus, two large complexes which expose large domains to opposite membrane surfaces exist in the inner membrane and interact with each other: the Phb1p-Phb2p complex with an apparent molecular mass of approximately 2 MDa, and the m-AAA protease with an apparent molecular mass of approximately 1 MDa....
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...They eluted in fractions corresponding to a native molecular mass of approximately 2 MDa under these conditions....
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...Upon determination of the native molecular mass of the m-AAA protease by gel filtration, strikingly different results were obtained in the presence of different detergents: when mitochondrial membranes were extracted with digitonin, the m-AAA protease subunits Yta10p and Yta12p eluted from the column in a single peak which corresponded to a molecular mass greater than 2 MDa (Fig....
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...Their catalytic sites, however, are exposed to opposite membrane surfaces: the m-AAA protease containing Yta10p (Afg3p) and Yta12p (Rca1p) acts on the matrix side, while the i-AAA protease containing Yme1p is active in the intermembrane space (3, 20)....
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...In contrast, after solubilization of mitochondria with the nonionic detergent Triton X-100, both m-AAA protease subunits coeluted from the sizing column in fractions corresponding to a native molecular mass of approximately 1 MDa as reported previously (Fig....
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310 citations
References
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