ArticleThe EMBO journal2010
Crystal structure of the human CNOT6L nuclease domain reveals strict poly(A) substrate specificity.
Article in The EMBO journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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Who cites it
64 citing papers in PubMed.
- Global Regulatory Functions of the Human CCR4-NOT Complex in mRNA Deadenylation and Decay.bioRxiv : the preprint server for biology · 2026Article
- Enhancing mRNA stability and translational potential through tailored modifications at the 3' end.RSC chemical biology · 2026Article
- CNOT6 deadenylase safeguards postnatal growth and metabolic transition viabioRxiv : the preprint server for biology · 2026Article
- Review
- The CCR4-NOT complex: a multifaceted sensor of molecular signals instructing eukaryotic mRNA translation and stability.Nucleic acids research · 2025Review
- Discovery of Drug-like Inhibitors of the Human Caf1/CNOT7 poly(A)-Selective Nuclease Using Compound Screening.Biomolecules · 2025Article
- Human CCR4 deadenylase homolog Angel1 is a non-stop mRNA decay factor.RNA (New York, N.Y.) · 2025Article
- Review
- Exploring the CNOT1(800-999) HEAT Domain and Its Interactions with Tristetraprolin (TTP) as Revealed by Hydrogen/Deuterium Exchange Mass Spectrometry.Biomolecules · 2025Article
- Deadenylation kinetics of mixed poly(A) tails at single-nucleotide resolution.Nature structural & molecular biology · 2024Article
- Structure and function of molecular machines involved in deadenylation-dependent 5'-3' mRNA degradation.Frontiers in genetics · 2023Review
- Regulation of eukaryotic mRNA deadenylation and degradation by the Ccr4-Not complex.Frontiers in cell and developmental biology · 2023Review
- Cytidine-containing tails robustly enhance and prolong protein production of synthetic mRNA in cell andMolecular therapy. Nucleic acids · 2022Article
- Regulation of the multisubunit CCR4-NOT deadenylase in the initiation of mRNA degradation.Current opinion in structural biology · 2022Review
- Biochemical and in silico identification of the active site and the catalytic mechanism of the circadian deadenylase HESPERIN.FEBS open bio · 2022Article
- Deadenylase-dependent mRNA decay of GDF15 and FGF21 orchestrates food intake and energy expenditure.Cell metabolism · 2022Article
- Structure of the human Ccr4-Not nuclease module using X-ray crystallography and electron paramagnetic resonance spectroscopy distance measurements.Protein science : a publication of the Protein Society · 2022Article
- Differential regulation of mRNA fate by the human Ccr4-Not complex is driven by coding sequence composition and mRNA localization.Genome biology · 2021Article
- Crystal structure and functional properties of the human CCR4-CAF1 deadenylase complex.Nucleic acids research · 2021Article
- tRNA 3' shortening by LCCR4 as a response to stress in Trypanosoma brucei.Nucleic acids research · 2021Article
4 more citing papers are in PubMed but not listed here.
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Authors and funding
12 authors.
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Abstract
CCR4, an evolutionarily conserved member of the CCR4-NOT complex, is the main cytoplasmic deadenylase. It contains a C-terminal nuclease domain with homology to the endonuclease-exonuclease-phosphatase (EEP) family of enzymes. We have determined the high-resolution three-dimensional structure of the nuclease domain of CNOT6L, a human homologue of CCR4, by X-ray crystallography using the single-wavelength anomalous dispersion method. This first structure of a deadenylase belonging to the EEP family adopts a complete alpha/beta sandwich fold typical of hydrolases with highly conserved active site residues similar to APE1. The active site of CNOT6L should recognize the RNA substrate through its negatively charged surface. In vitro deadenylase assays confirm the critical active site residues and show that the nuclease domain of CNOT6L exhibits full Mg(2+)-dependent deadenylase activity with strict poly(A) RNA substrate specificity. To understand the structural basis for poly(A) RNA substrate binding, crystal structures of the CNOT6L nuclease domain have also been determined in complex with AMP and poly(A) DNA. The resulting structures suggest a molecular deadenylase mechanism involving a pentacovalent phosphate transition.
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