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First published online 23 April 2008
doi: 10.1242/dev.021444

Development 135, 1969-1979 (2008)
Published by The Company of Biologists 2008
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PAP- and GLD-2-type poly(A) polymerases are required sequentially in cytoplasmic polyadenylation and oogenesis in Drosophila

Perrine Benoit1, Catherine Papin1, Jae Eun Kwak2, Marvin Wickens2 and Martine Simonelig1,*

1 mRNA Regulation and Development, Institut de Génétique Humaine, CNRS UPR 1142, 141 rue de la Cardonille, 34396 Montpellier Cedex 5, France.
2 Department of Biochemistry, 433 Babcock Drive, University of Wisconsin, Madison, WI 53706 1544, USA.

* Author for correspondence (e-mail: Martine.Simonelig{at}igh.cnrs.fr)

Accepted 8 April 2008

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.

Key words: Cytoplasmic polyadenylation, Drosophila, GLD-2, Meiosis, Metaphase I, Translational control


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