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pubmed-article:2174423pubmed:abstractTextIn the ubiquitin pathway for intracellular protein breakdown, proteins ligated to ubiquitin are degraded by a large (26 S) ATP-dependent protease complex. It was found previously that the 26 S complex is assembled from three different enzyme components by a process that requires MgATP. In addition, MgATP is also required for the continued action of the 26 S complex in the breakdown of ubiquitin-protein conjugates. In the present study we have tried to gain some insight into the mode of action of ATP by following ATP hydrolysis by the 26 S complex and its three components. It was found that none of the three unassembled components had significant ATPase activity, but such activity appeared following their entry into the 26 S complex. The presence of all three components and of MgATP was required for the formation of complex-associated ATPase activity. GTP and UTP cannot replace ATP for complex assembly, but these nucleotides can substitute for ATP in the stimulation of the conjugate-degrading activity of the 26 S complex. Unlabeled GTP and UTP inhibit the hydrolysis of [gamma-32P] ATP by complex-associated ATPase, indicating that this activity is related to the latter site of ATP action in this system.lld:pubmed
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pubmed-article:2174423pubmed:articleTitleAssembly of the 26 S complex that degrades proteins ligated to ubiquitin is accompanied by the formation of ATPase activity.lld:pubmed
pubmed-article:2174423pubmed:affiliationUnit of Biochemistry, Faculty of Medicine, Technion-Israel Institute of Technology, Haifa.lld:pubmed
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pubmed-article:2174423pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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