Evolution from covalent conjugation to non-covalent interaction in the ubiquitin-like ATG12 system
| Autor: | Yoshitaka Kurikawa, Hirokazu Sakamoto, Nobuo N. Noda, Yasuyoshi Sakai, Honglin Jia, Joe Kimanthi Mutungi, Masahide Oku, Hayashi Yamamoto, Yu Pang, Noboru Mizushima, Mayurbhai Himatbhai Sahani, Kiyoshi Kita |
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| Rok vydání: | 2019 |
| Předmět: |
0303 health sciences
biology Stereochemistry Chemistry ATG5 Substrate (chemistry) Conjugated system biology.organism_classification Yeast Pichia pastoris ATG12 03 medical and health sciences 0302 clinical medicine Ubiquitin Structural Biology Covalent bond biology.protein Molecular Biology 030217 neurology & neurosurgery 030304 developmental biology |
| Zdroj: | Nature Structural & Molecular Biology. 26:289-296 |
| ISSN: | 1545-9985 1545-9993 |
| DOI: | 10.1038/s41594-019-0204-3 |
| Popis: | Ubiquitin or ubiquitin-like proteins can be covalently conjugated to multiple proteins that do not necessarily have binding interfaces. Here, we show that an evolutionary transition from covalent conjugation to non-covalent interaction has occurred in the ubiquitin-like autophagy-related 12 (ATG12) conjugation system. ATG12 is covalently conjugated to its sole substrate, ATG5, by a ubiquitylation-like mechanism. However, the apicomplexan parasites Plasmodium and Toxoplasma and some yeast species such as Komagataella phaffii (previously Pichia pastoris) lack the E2-like enzyme ATG10 and the most carboxy (C)-terminal glycine of ATG12, both of which are required for covalent linkage. Instead, ATG12 in these organisms forms a non-covalent complex with ATG5. This non-covalent ATG12-ATG5 complex retains the ability to facilitate ATG8-phosphatidylethanolamine conjugation. These results suggest that ubiquitin-like covalent conjugation can evolve to a simpler non-covalent interaction, most probably when the system has a limited number of targets. |
| Databáze: | OpenAIRE |
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