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Conformational transition of the lid helix covering the protease active site is essential for the ATP-dependent protease activity of FtsH |
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| Authors: | Ryoji SunoMasakazu Shimoyama Akiko AbeTatsuro Shimamura Natsuka ShimodateYo-hei Watanabe Yoshinori AkiyamaMasasuke Yoshida |
| Affiliation: | a Department of Molecular Bioscience, Faculty of Life Sciences, Kyoto Sangyo University, Kyoto 603-8555, Japan b Chemical Resources Laboratory, Tokyo Institute of Technology, 4259 Nagatsuta, Yokohama 226-8503, Japan c Institute for Virus Research, Kyoto University, Kyoto 606-8507, Japan d Department of Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto 606-8501, Japan e Department of Biology, Faculty of Science and Engineering, Konan University, Okamoto 8-9-1, Kobe 658-8501, Japan |
| Abstract: | When bound to ADP, ATP-dependent protease FtsH subunits adopt either an “open” or “closed” conformation. In the open state, the protease catalytic site is located in a narrow space covered by a lid-like helix. This space disappears in the closed form because the lid helix bends at Gly448. Here, we replaced Gly448 with various residues that stabilize helices. Most mutants retained low ATPase activity and bound to the substrate protein, but lost protease activity. However, a mutant proline substitution lost both activities. Our study shows that the conformational transition of the lid helix is essential for the function of FtsH.Structured summary of protein interactionsFtsH and FtsHbind by molecular sieving (View Interaction) |
| Keywords: | FtsH AAA+ ATP-dependent protease Protease ATPase |
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