ArticleDevelopmental biology2012
Xenopus laevis zygote arrest 2 (zar2) encodes a zinc finger RNA-binding protein that binds to the translational control sequence in the maternal Wee1 mRNA and regulates translation.
Article in Developmental biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 31 citations in OpenAlex.
- Attribute Network-based Ranking (ANeR) identifies conserved translational fingerprints of M-phase.Nucleic acids research · 2026Article
- Decoding protein phosphorylation during oocyte meiotic divisions using phosphoproteomics.eLife · 2025Article
- ZAR1 and ZAR2 orchestrate the dynamics of maternal mRNA polyadenylation during mouse oocyte development.Genome biology · 2025Article
- A genome-wide perspective of the maternal mRNA translation program during oocyte development.Seminars in cell & developmental biology · 2024Review
- Multiple intersecting pathways are involved in the phosphorylation of CPEB1 to activate translation during mouse oocyte meiosis.bioRxiv : the preprint server for biology · 2024Article
- Revisiting ZAR proteins: the understudied regulator of female fertility and beyond.Cellular and molecular life sciences : CMLS · 2022Review
- RTP4 Is a Potent IFN-Inducible Anti-flavivirus Effector Engaged in a Host-Virus Arms Race in Bats and Other Mammals.Cell host & microbe · 2020Article
- Translational Control ofCells · 2020Review
- ZAR1 and ZAR2 are required for oocyte meiotic maturation by regulating the maternal transcriptome and mRNA translational activation.Nucleic acids research · 2019Article
- Acquisition of oocyte competence to develop as an embryo: integrated nuclear and cytoplasmic events.Human reproduction update · 2018Review
- ZAR1 knockdown promotes the differentiation of human neuroblastoma cells by suppression of MYCN expression.Medical oncology (Northwood, London, England) · 2017Article
- Insertion of inter-domain linkers improves expression and bioactivity of Zygote arrest (Zar) fusion proteins.Protein engineering, design & selection : PEDS · 2017Article
- Functional Integration of mRNA Translational Control Programs.Biomolecules · 2015Review
- Zar1 represses translation in Xenopus oocytes and binds to the TCS in maternal mRNAs with different characteristics than Zar2.Biochimica et biophysica acta · 2013Article
- Specificity factors in cytoplasmic polyadenylation.Wiley interdisciplinary reviews. RNAReview
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11 authors at 4 institutions in 1 country.
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Abstract
Zygote arrest (Zar) proteins are crucial for early embryonic development, but their molecular mechanism of action is unknown. The Translational Control Sequence (TCS) in the 3' untranslated region (UTR) of the maternal mRNA, Wee1, mediates translational repression in immature Xenopus oocytes and translational activation in mature oocytes, but the protein that binds to the TCS and mediates translational control is not known. Here we show that Xenopus laevis Zar2 (encoded by zar2) binds to the TCS in maternal Wee1 mRNA and represses translation in immature oocytes. Using yeast 3 hybrid assays and electrophoretic mobility shift assays, Zar2 was shown to bind specifically to the TCS in the Wee1 3'UTR. RNA binding required the presence of Zn(2+) and conserved cysteines in the C-terminal domain, suggesting that Zar2 contains a zinc finger. Consistent with regulating maternal mRNAs, Zar2 was present throughout oogenesis, and endogenous Zar2 co-immunoprecipitated endogenous Wee1 mRNA from immature oocytes, demonstrating the physiological significance of the protein-RNA interaction. Interestingly, Zar2 levels decreased during oocyte maturation. Dual luciferase reporter tethered assays showed that Zar2 repressed translation in immature oocytes. Translational repression was relieved during oocyte maturation and this coincided with degradation of Zar2 during maturation. This is the first report of a molecular function of zygote arrest proteins. These data show that Zar2 contains a zinc finger and is a trans-acting factor for the TCS in maternal mRNAs in immature Xenopus oocytes.
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