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Updated: Jul 5, 2026

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Published on: January 12, 2024
PAP- and GLD-2-type poly(A) polymerases are required sequentially in cytoplasmic polyadenylation and oogenesis in
Perrine Benoit1, Catherine Papin, Jae Eun Kwak
1mRNA Regulation and Development, Institut de Génétique Humaine, CNRS UPR 1142, 141 rue de la Cardonille, 34396 Montpellier Cedex 5, France.
Insights
Two distinct poly(A) polymerases, Wispy (a GLD-2 type) and canonical PAP, regulate cytoplasmic polyadenylation in Drosophila oogenesis. Wispy is crucial for later stages, while PAP is essential for earlier steps, both interacting with Orb.
Area of Science:
- Developmental Biology
- Molecular Biology
- Genetics
Background:
- Cytoplasmic polyadenylation is vital for activating maternal mRNA translation during early development.
- In vertebrates, this process involves CPEB and the GLD-2 poly(A) polymerase.
- Canonical poly(A) polymerases (PAPs) are distinct from GLD-2 type polymerases.
Purpose of the Study:
- To investigate the role of the GLD-2 type poly(A) polymerase in Drosophila oogenesis.
- To determine the specific functions of Wispy and canonical PAP in relation to oogenesis stages and the CPEB protein Orb.
Main Methods:
- Utilized tethering assays and in vivo studies to assess Wispy's poly(A) polymerase activity.
- Conducted genetic interaction studies to analyze the interplay between Wispy, PAP, and Orb.
- Performed co-immunoprecipitation to investigate physical interactions within an ovarian complex.
Main Results:
- Identified Wispy as the Drosophila GLD-2 type poly(A) polymerase in the female germline.
- Demonstrated Wispy's role in cytoplasmic polyadenylation of specific mRNAs during late oogenesis and early embryogenesis.
- Showed Wispy is essential for meiotic arrest and progression, while canonical PAP functions in earlier oogenesis stages.
- Confirmed both Wispy and PAP interact genetically and physically with Orb.
Conclusions:
- Two distinct poly(A) polymerases, Wispy and canonical PAP, operate in the female germline for cytoplasmic polyadenylation.
- Each polymerase is specifically required for different, sequential stages of oogenesis.
- Wispy and PAP function in a complex with Orb, highlighting a coordinated regulatory mechanism.
Abstract:
Cytoplasmic polyadenylation has an essential role in activating maternal mRNA translation during early development. In vertebrates, the reaction requires CPEB, an RNA-binding protein and the poly(A) polymerase GLD-2. GLD-2-type poly(A) polymerases form a family clearly distinguishable from canonical poly(A) polymerases (PAPs). In Drosophila, canonical PAP is involved in cytoplasmic polyadenylation with Orb, the Drosophila CPEB, during mid-oogenesis. We show that the female germline GLD-2 is encoded by wispy. Wispy acts as a poly(A) polymerase in a tethering assay and in vivo for cytoplasmic polyadenylation of specific mRNA targets during late oogenesis and early embryogenesis. wispy function is required at the final stage of oogenesis for metaphase of meiosis I arrest and for progression beyond this stage. By contrast, canonical PAP acts with Orb for the earliest steps of oogenesis. Both Wispy and PAP interact with Orb genetically and physically in an ovarian complex. We conclude that two distinct poly(A) polymerases have a role in cytoplasmic polyadenylation in the female germline, each of them being specifically required for different steps of oogenesis.
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