Document Detail


Noncanonical recognition and UBL loading of distinct E2s by autophagy-essential Atg7.
MedLine Citation:
PMID:  23142983     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
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.
Authors:
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:
Type:  JOURNAL ARTICLE     Date:  2012-11-11
Journal Detail:
Title:  Nature structural & molecular biology     Volume:  -     ISSN:  1545-9985     ISO Abbreviation:  Nat. Struct. Mol. Biol.     Publication Date:  2012 Nov 
Date Detail:
Created Date:  2012-11-12     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101186374     Medline TA:  Nat Struct Mol Biol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
1] Department of Structural Biology, Faculty of Advanced Life Science, Hokkaido University, Sapporo, Japan. [2].
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