Not4-dependent targeting of MMF1 mRNA to mitochondria limits its expression via ribosome pausing, Egd1 ubiquitination, Caf130, no-go-decay and autophagy

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Název: Not4-dependent targeting of MMF1 mRNA to mitochondria limits its expression via ribosome pausing, Egd1 ubiquitination, Caf130, no-go-decay and autophagy
Autoři: Chen, Siyu, Allen, George Edward, Panasenko, Olesya, Collart, Martine
Zdroj: Nucleic Acids Res
Informace o vydavateli: Oxford University Press (OUP), 2023.
Rok vydání: 2023
Témata: Autophagy / genetics, Saccharomyces cerevisiae Proteins, RNA, Messenger / metabolism, Ribosomes / metabolism, Saccharomyces cerevisiae, Ribosomes / genetics, Mitochondrial Proteins, Saccharomyces cerevisiae Proteins / genetics, Autophagy, Saccharomyces cerevisiae / metabolism, RNA, Messenger, Mitochondrial Proteins / genetics, Molecular Biology, Saccharomyces cerevisiae Proteins / metabolism, Membrane Proteins / genetics, RNA, Messenger / genetics, Mitochondria / metabolism, Ubiquitination, Membrane Proteins, Mitochondria, Mitochondria / genetics, Mitochondrial Proteins / metabolism, Saccharomyces cerevisiae / genetics, Ribosomes
Popis: The Ccr4–Not complex is a conserved multi protein complex with diverse roles in the mRNA life cycle. Recently we determined that the Not1 and Not4 subunits of Ccr4–Not inversely regulate mRNA solubility and thereby impact dynamics of co-translation events. One mRNA whose solubility is limited by Not4 is MMF1 encoding a mitochondrial matrix protein. In this work we uncover a mechanism that limits MMF1 overexpression and depends upon its co-translational targeting to the mitochondria. We have named this mechanism Mito-ENCay. This mechanism relies on Not4 promoting ribosome pausing during MMF1 translation, and hence the co-translational docking of the MMF1 mRNA to mitochondria via the mitochondrial targeting sequence of the Mmf1 nascent chain, the Egd1 chaperone, the Om14 mitochondrial outer membrane protein and the co-translational import machinery. Besides co-translational Mitochondrial targeting, Mito-ENCay depends upon Egd1 ubiquitination by Not4, the Caf130 subunit of the Ccr4–Not complex, the mitochondrial outer membrane protein Cis1, autophagy and no-go-decay.
Druh dokumentu: Article
Conference object
Other literature type
Popis souboru: application/pdf
Jazyk: English
ISSN: 1362-4962
0305-1048
DOI: 10.1093/nar/gkad299
Přístupová URL adresa: https://pubmed.ncbi.nlm.nih.gov/37094076
https://archive-ouverte.unige.ch/unige:172792
https://doi.org/10.1093/nar/gkad299
Rights: CC BY
URL: http://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
Přístupové číslo: edsair.doi.dedup.....1d1d27051e407de4e83c6647c35eeb00
Databáze: OpenAIRE
Popis
Abstrakt:The Ccr4–Not complex is a conserved multi protein complex with diverse roles in the mRNA life cycle. Recently we determined that the Not1 and Not4 subunits of Ccr4–Not inversely regulate mRNA solubility and thereby impact dynamics of co-translation events. One mRNA whose solubility is limited by Not4 is MMF1 encoding a mitochondrial matrix protein. In this work we uncover a mechanism that limits MMF1 overexpression and depends upon its co-translational targeting to the mitochondria. We have named this mechanism Mito-ENCay. This mechanism relies on Not4 promoting ribosome pausing during MMF1 translation, and hence the co-translational docking of the MMF1 mRNA to mitochondria via the mitochondrial targeting sequence of the Mmf1 nascent chain, the Egd1 chaperone, the Om14 mitochondrial outer membrane protein and the co-translational import machinery. Besides co-translational Mitochondrial targeting, Mito-ENCay depends upon Egd1 ubiquitination by Not4, the Caf130 subunit of the Ccr4–Not complex, the mitochondrial outer membrane protein Cis1, autophagy and no-go-decay.
ISSN:13624962
03051048
DOI:10.1093/nar/gkad299