期刊
CELL REPORTS
卷 31, 期 12, 页码 -出版社
CELL PRESS
DOI: 10.1016/j.celrep.2020.107783
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资金
- Ontario Graduate Scholarship
- University of Toronto Open Scholarships
- Canadian Institutes of Health Research [PJT-159702]
- Natural Sciences and Engineering Research Council of Canada
- Deutsche Forschungsgemeinschaft [WA 548/17-1, SPP 1935]
- National Institutes of Health [R35GM128813, T32GM007388]
In animal embryos, the matemal-to-zygotic transition (MZT) hands developmental control from maternal to zygotic gene products. We show that the maternal proteome represents more than half of the protein-coding capacity of Drosophila melanogaster's genome, and that 2% of this proteome is rapidly degraded during the MZT. Cleared proteins include the post-transcriptional repressors Cup, Trailer hitch (TRAL), Maternal expression at 31B (ME31B), and Smaug (SMG). Although the ubiquitin-proteasome system is necessary for clearance of these repressors, distinct E3 ligase complexes target them: the C-terminal to Lis1 Homology (CTLH) complex targets Cup, TRAL, and ME31B for degradation early in the MZT and the Skp/Cullin/Fbox-containing (SCF) complex targets SMG at the end of the MZT. Deleting the C-terminal 233 amino acids of SMG abrogates F-box protein interaction and confers immunity to degradation. Persistent SMG downregulates zygotic re-expression of mRNAs whose maternal contribution is degraded by SMG. Thus, clearance of SMG permits an orderly MZT.
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