ArticleThe Biochemical journal2015
The enzyme activities of Caf1 and Ccr4 are both required for deadenylation by the human Ccr4-Not nuclease module.
Article in The Biochemical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 35 citations in OpenAlex.
- Discovery of Drug-like Inhibitors of the Human Caf1/CNOT7 poly(A)-Selective Nuclease Using Compound Screening.Biomolecules · 2025Article
- Discovery of Substituted 5-(2-Hydroxybenzoyl)-2-Pyridone Analogues as Inhibitors of the Human Caf1/CNOT7 Ribonuclease.Molecules (Basel, Switzerland) · 2024Article
- Quantitative Biochemical Analysis of Deadenylase Enzymes Using Fluorescence and Chemiluminescence-Based Assays.Methods in molecular biology (Clifton, N.J.) · 2024Article
- RNA binding proteins Smaug and Cup induce CCR4-NOT-dependent deadenylation of the nanos mRNA in a reconstituted system.Nucleic acids research · 2023Article
- 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
- Processing body (P-body) and its mediators in cancer.Molecular and cellular biochemistry · 2022Review
- 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
- Crystal structure and functional properties of the human CCR4-CAF1 deadenylase complex.Nucleic acids research · 2021Article
- The Arabidopsis NOT4A E3 ligase promotes PGR3 expression and regulates chloroplast translation.Nature communications · 2021Article
- Importance of CNOT8 Deadenylase Subunit in DNA Damage Responses Following Ionizing Radiation (IR).Reports of biochemistry & molecular biology · 2020Article
- A low-complexity region in human XRN1 directly recruits deadenylation and decapping factors in 5'-3' messenger RNA decay.Nucleic acids research · 2019Article
- DEAD-box helicase eIF4A2 inhibits CNOT7 deadenylation activity.Nucleic acids research · 2019Article
- Role of the Citrus sinensis RNA deadenylase CsCAF1 in citrus canker resistance.Molecular plant pathology · 2019Article
- Reconstitution of recombinant human CCR4-NOT reveals molecular insights into regulated deadenylation.Nature communications · 2019Article
- 1-Hydroxy-xanthine derivatives inhibit the human Caf1 nuclease and Caf1-containing nuclease complexes via MgFEBS open bio · 2019Article
- The Interplay between the RNA Decay and Translation Machinery in Eukaryotes.Cold Spring Harbor perspectives in biology · 2018Review
- ATP is dispensable for both miRNA- and Smaug-mediated deadenylation reactions.RNA (New York, N.Y.) · 2017Article
- Reconstitution of Targeted Deadenylation by the Ccr4-Not Complex and the YTH Domain Protein Mmi1.Cell reports · 2016Article
- CCR4 and CAF1 deadenylases have an intrinsic activity to remove the post-poly(A) sequence.RNA (New York, N.Y.) · 2016Article
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
In eukaryotic cells, the shortening and removal of the poly(A) tail (deadenylation) of cytoplasmic mRNA is a key event in regulated mRNA degradation. A major enzyme involved in deadenylation is the Ccr4-Not deadenylase complex, which can be recruited to its target mRNA by RNA-binding proteins or the miRNA repression complex. In addition to six non-catalytic components, the complex contains two enzymatic subunits with ribonuclease activity: Ccr4 and Caf1 (Pop2). In vertebrates, each deadenylase subunit is encoded by two paralogues: Caf1, which can interact with the anti-proliferative protein BTG2, is encoded by CNOT7 and CNOT8, whereas Ccr4 is encoded by the highly similar genes CNOT6 and CNOT6L. Currently, it is unclear whether the catalytic subunits work co-operatively or whether the nuclease components have unique roles in deadenylation. We therefore developed a method to express and purify a minimal human BTG2-Caf1-Ccr4 nuclease sub-complex from bacterial cells. By using chemical inhibition and well-characterized inactivating amino acid substitutions, we demonstrate that the enzyme activities of Caf1 and Ccr4 are both required for deadenylation in vitro. These results indicate that Caf1 and Ccr4 cooperate in mRNA deadenylation and suggest that the enzyme activities of Caf1 and Ccr4 are regulated via allosteric interactions within the nuclease module.
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