Atg7 Activates an Autophagy-Essential Ubiquitin-like Protein Atg8 through Multi-Step Recognition
In: Journal of molecular biology, Jg. 430 (2017-09-17), Heft 3
Online
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Zugriff:
Atg8 is a unique ubiquitin-like protein that is covalently conjugated with a phosphatidylethanolamine through reactions similar to ubiquitination and plays essential roles in autophagy. Atg7 is the E1 enzyme for Atg8, and it activates the C-terminal Gly116 of Atg8 using ATP. Here, we report the crystal structure of Atg8 bound to the C-terminal domain of Atg7 in an unprecedented mode. Atg8 neither contacts with the central β-sheet nor binds to the catalytic site of Atg7, both of which were observed in previously reported Atg7-Atg8 structures. Instead, Atg8 binds to the C-terminal α-helix and crossover loop, thereby changing the autoinhibited conformation of the crossover loop observed in the free Atg7 structure into a short helix and a disordered loop. Mutational analyses suggested that this interaction mode is important for the activation reaction. We propose that Atg7 recognizes Atg8 through multiple steps, which would be necessary to induce a conformational change in Atg7 that is optimal for the activation reaction.
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Atg7 Activates an Autophagy-Essential Ubiquitin-like Protein Atg8 through Multi-Step Recognition
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Autor/in / Beteiligte Person: | Ohsumi, Yoshinori ; Inagaki, Fuyuhiko ; Fujioka, Yuko ; Satoo, Kenji ; Noda, Nobuo N. ; Yamaguchi, Masaya ; Suzuki, Hironori |
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Zeitschrift: | Journal of molecular biology, Jg. 430 (2017-09-17), Heft 3 |
Veröffentlichung: | 2017 |
Medientyp: | unknown |
ISSN: | 1089-8638 (print) |
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