Specific recognition and ubiquitination of translating ribosomes by mammalian CCR4–NOT

Translation affects messenger RNA stability and, in yeast, this is mediated by the Ccr4–Not deadenylation complex. The details of this process in mammals remain unclear. Here, we use cryogenic electron microscopy (cryo-EM) and crosslinking mass spectrometry to show that mammalian CCR4–NOT specifical...

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Vydáno v:	Nature structural & molecular biology Ročník 30; číslo 9; s. 1314 - 1322
Hlavní autoři:	Absmeier, Eva, Chandrasekaran, Viswanathan, O’Reilly, Francis J., Stowell, James A. W., Rappsilber, Juri, Passmore, Lori A.
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	New York Nature Publishing Group US 01.09.2023 Nature Publishing Group
Témata:	631/337/1645 631/337/1645/2020 631/337/574 631/337/574/1789 631/535/1258/1259 Animals Biochemistry Biological Microscopy Biomedical and Life Sciences Conformation Crosslinking E coli Electron microscopy Elongation Humans Inserts Life Sciences Mammals Mass Spectrometry Mass spectroscopy Membrane Biology Molecular biology mRNA stability mRNA turnover Polypeptides Protein Structure Proteins Rabbits Receptors, CCR4 Ribonucleases Ribosomes Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Stability Stalling Sucrose Transcription Factors Transfer RNA Translation elongation Translations Ubiquitin Ubiquitination Yeast
ISSN:	1545-9993, 1545-9985, 1545-9985
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Abstract	Translation affects messenger RNA stability and, in yeast, this is mediated by the Ccr4–Not deadenylation complex. The details of this process in mammals remain unclear. Here, we use cryogenic electron microscopy (cryo-EM) and crosslinking mass spectrometry to show that mammalian CCR4–NOT specifically recognizes ribosomes that are stalled during translation elongation in an in vitro reconstituted system with rabbit and human components. Similar to yeast, mammalian CCR4–NOT inserts a helical bundle of its CNOT3 subunit into the empty E site of the ribosome. Our cryo-EM structure shows that CNOT3 also locks the L1 stalk in an open conformation to inhibit further translation. CCR4–NOT is required for stable association of the nonconstitutive subunit CNOT4, which ubiquitinates the ribosome, likely to signal stalled translation elongation. Overall, our work shows that human CCR4–NOT not only detects but also enforces ribosomal stalling to couple translation and mRNA decay. Using cryo-EM, the authors show that the mammalian CCR4–NOT complex specifically recognizes stalled translating ribosomes similar to the yeast complex, locks them in a translation-incompetent state and coordinates their ubiquitylation, highlighting its central role in linking translation to mRNA stability.
AbstractList	Translation affects messenger RNA stability and, in yeast, this is mediated by the Ccr4-Not deadenylation complex. The details of this process in mammals remain unclear. Here, we use cryogenic electron microscopy (cryo-EM) and crosslinking mass spectrometry to show that mammalian CCR4-NOT specifically recognizes ribosomes that are stalled during translation elongation in an in vitro reconstituted system with rabbit and human components. Similar to yeast, mammalian CCR4-NOT inserts a helical bundle of its CNOT3 subunit into the empty E site of the ribosome. Our cryo-EM structure shows that CNOT3 also locks the L1 stalk in an open conformation to inhibit further translation. CCR4-NOT is required for stable association of the nonconstitutive subunit CNOT4, which ubiquitinates the ribosome, likely to signal stalled translation elongation. Overall, our work shows that human CCR4-NOT not only detects but also enforces ribosomal stalling to couple translation and mRNA decay. Translation affects messenger RNA stability and, in yeast, this is mediated by the Ccr4–Not deadenylation complex. The details of this process in mammals remain unclear. Here, we use cryogenic electron microscopy (cryo-EM) and crosslinking mass spectrometry to show that mammalian CCR4–NOT specifically recognizes ribosomes that are stalled during translation elongation in an in vitro reconstituted system with rabbit and human components. Similar to yeast, mammalian CCR4–NOT inserts a helical bundle of its CNOT3 subunit into the empty E site of the ribosome. Our cryo-EM structure shows that CNOT3 also locks the L1 stalk in an open conformation to inhibit further translation. CCR4–NOT is required for stable association of the nonconstitutive subunit CNOT4, which ubiquitinates the ribosome, likely to signal stalled translation elongation. Overall, our work shows that human CCR4–NOT not only detects but also enforces ribosomal stalling to couple translation and mRNA decay.Using cryo-EM, the authors show that the mammalian CCR4–NOT complex specifically recognizes stalled translating ribosomes similar to the yeast complex, locks them in a translation-incompetent state and coordinates their ubiquitylation, highlighting its central role in linking translation to mRNA stability. Translation affects messenger RNA stability and, in yeast, this is mediated by the Ccr4–Not deadenylation complex. The details of this process in mammals remain unclear. Here, we use cryogenic electron microscopy (cryo-EM) and crosslinking mass spectrometry to show that mammalian CCR4–NOT specifically recognizes ribosomes that are stalled during translation elongation in an in vitro reconstituted system with rabbit and human components. Similar to yeast, mammalian CCR4–NOT inserts a helical bundle of its CNOT3 subunit into the empty E site of the ribosome. Our cryo-EM structure shows that CNOT3 also locks the L1 stalk in an open conformation to inhibit further translation. CCR4–NOT is required for stable association of the nonconstitutive subunit CNOT4, which ubiquitinates the ribosome, likely to signal stalled translation elongation. Overall, our work shows that human CCR4–NOT not only detects but also enforces ribosomal stalling to couple translation and mRNA decay. Using cryo-EM, the authors show that the mammalian CCR4–NOT complex specifically recognizes stalled translating ribosomes similar to the yeast complex, locks them in a translation-incompetent state and coordinates their ubiquitylation, highlighting its central role in linking translation to mRNA stability. Translation impacts mRNA stability and, in yeast, this is mediated by the Ccr4-Not deadenylation complex. The details of this process in mammals remain unclear. Here, we use cryoEM and crosslinking mass spectrometry to show that mammalian CCR4-NOT specifically recognizes ribosomes that are stalled during translation elongation in an in vitro reconstituted system. Similar to yeast, CCR4-NOT inserts a helical bundle of its CNOT3 subunit into the empty E site of the ribosome. Our cryoEM structure shows that human CNOT3 also locks the L1 stalk in an open conformation to inhibit further translation. CCR4-NOT is required for stable association of the non-constitutive subunit CNOT4, which ubiquitinates the ribosome, likely to signal stalled translation elongation. Overall, our work shows that human CCR4-NOT not only detects but also enforces ribosomal stalling to couple translation and mRNA decay. Translation affects messenger RNA stability and, in yeast, this is mediated by the Ccr4-Not deadenylation complex. The details of this process in mammals remain unclear. Here, we use cryogenic electron microscopy (cryo-EM) and crosslinking mass spectrometry to show that mammalian CCR4-NOT specifically recognizes ribosomes that are stalled during translation elongation in an in vitro reconstituted system with rabbit and human components. Similar to yeast, mammalian CCR4-NOT inserts a helical bundle of its CNOT3 subunit into the empty E site of the ribosome. Our cryo-EM structure shows that CNOT3 also locks the L1 stalk in an open conformation to inhibit further translation. CCR4-NOT is required for stable association of the nonconstitutive subunit CNOT4, which ubiquitinates the ribosome, likely to signal stalled translation elongation. Overall, our work shows that human CCR4-NOT not only detects but also enforces ribosomal stalling to couple translation and mRNA decay.Translation affects messenger RNA stability and, in yeast, this is mediated by the Ccr4-Not deadenylation complex. The details of this process in mammals remain unclear. Here, we use cryogenic electron microscopy (cryo-EM) and crosslinking mass spectrometry to show that mammalian CCR4-NOT specifically recognizes ribosomes that are stalled during translation elongation in an in vitro reconstituted system with rabbit and human components. Similar to yeast, mammalian CCR4-NOT inserts a helical bundle of its CNOT3 subunit into the empty E site of the ribosome. Our cryo-EM structure shows that CNOT3 also locks the L1 stalk in an open conformation to inhibit further translation. CCR4-NOT is required for stable association of the nonconstitutive subunit CNOT4, which ubiquitinates the ribosome, likely to signal stalled translation elongation. Overall, our work shows that human CCR4-NOT not only detects but also enforces ribosomal stalling to couple translation and mRNA decay.
Author	Stowell, James A. W. Passmore, Lori A. O’Reilly, Francis J. Absmeier, Eva Chandrasekaran, Viswanathan Rappsilber, Juri
AuthorAffiliation	3 Wellcome Centre for Cell Biology, University of Edinburgh, Edinburgh UK 2 Technische Universität Berlin, Chair of Bioanalytics, 10623 Berlin, Germany 1 MRC Laboratory of Molecular Biology, Cambridge UK
AuthorAffiliation_xml	– name: 2 Technische Universität Berlin, Chair of Bioanalytics, 10623 Berlin, Germany – name: 1 MRC Laboratory of Molecular Biology, Cambridge UK – name: 3 Wellcome Centre for Cell Biology, University of Edinburgh, Edinburgh UK
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Snippet	Translation affects messenger RNA stability and, in yeast, this is mediated by the Ccr4–Not deadenylation complex. The details of this process in mammals... Translation affects messenger RNA stability and, in yeast, this is mediated by the Ccr4-Not deadenylation complex. The details of this process in mammals... Translation impacts mRNA stability and, in yeast, this is mediated by the Ccr4-Not deadenylation complex. The details of this process in mammals remain...
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SubjectTerms	631/337/1645 631/337/1645/2020 631/337/574 631/337/574/1789 631/535/1258/1259 Animals Biochemistry Biological Microscopy Biomedical and Life Sciences Conformation Crosslinking E coli Electron microscopy Elongation Humans Inserts Life Sciences Mammals Mass Spectrometry Mass spectroscopy Membrane Biology Molecular biology mRNA stability mRNA turnover Polypeptides Protein Structure Proteins Rabbits Receptors, CCR4 Ribonucleases Ribosomes Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Stability Stalling Sucrose Transcription Factors Transfer RNA Translation elongation Translations Ubiquitin Ubiquitination Yeast
Title	Specific recognition and ubiquitination of translating ribosomes by mammalian CCR4–NOT
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