| Noncanonical recognition and UBL loading of distinct E2s by autophagy-essential Atg7. | |
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MedLine Citation:
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PMID: 23142983 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Autophagy requires ubiquitin-like Atg8 and Atg12 conjugation systems, where Atg7 has a critical role as the sole E1 enzyme. Although Atg7 recognizes two distinct E2s, Atg3 and Atg10, it is not understood how Atg7 correctly loads these E2s with their cognate ubiquitin-like proteins, Atg8 and Atg12. Here, we report the crystal structures of the N-terminal domain of Atg7 bound to Atg10 or Atg3 of thermotolerant yeast and plant homologs. The observed Atg7-Atg10 and Atg7-Atg3 interactions, which resemble each other but are quite distinct from the canonical E1-E2 interaction, makes Atg7 suitable for transferring Atg12 to Atg10 and Atg8 to Atg3 by a trans mechanism. Notably, in vitro experiments showed that Atg7 loads Atg3 and Atg10 with Atg8 and Atg12 in a nonspecific manner, which suggests that cognate conjugate formation in vivo is not an intrinsic quality of Atg7. |
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Authors:
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Masaya Yamaguchi; Kazuaki Matoba; Ryoko Sawada; Yuko Fujioka; Hitoshi Nakatogawa; Hayashi Yamamoto; Yoshihiro Kobashigawa; Hisashi Hoshida; Rinji Akada; Yoshinori Ohsumi; Nobuo N Noda; Fuyuhiko Inagaki |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-11-11 |
Journal Detail:
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Title: Nature structural & molecular biology Volume: - ISSN: 1545-9985 ISO Abbreviation: Nat. Struct. Mol. Biol. Publication Date: 2012 Nov |
Date Detail:
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Created Date: 2012-11-12 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101186374 Medline TA: Nat Struct Mol Biol Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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1] Department of Structural Biology, Faculty of Advanced Life Science, Hokkaido University, Sapporo, Japan. [2]. |
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