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Wispy, the Drosophila homolog of GLD-2, is required during oogenesis and egg activation.
- Source :
-
Genetics [Genetics] 2008 Apr; Vol. 178 (4), pp. 2017-29. - Publication Year :
- 2008
-
Abstract
- Egg activation is the process that modifies mature, arrested oocytes so that embryo development can proceed. One key aspect of egg activation is the cytoplasmic polyadenylation of certain maternal mRNAs to permit or enhance their translation. wispy (wisp) maternal-effect mutations in Drosophila block development during the egg-to-embryo transition. We show here that the wisp gene encodes a member of the GLD-2 family of cytoplasmic poly(A) polymerases (PAPs). The WISP protein is required for poly(A) tail elongation of bicoid, Toll, and torso mRNAs upon egg activation. In Drosophila, WISP and Smaug (SMG) have previously been reported to be required to trigger the destabilization of maternal mRNAs during egg activation. SMG is the major regulator of this activity. We report here that SMG is still translated in activated eggs from wisp mutant mothers, indicating that WISP does not regulate mRNA stability by controlling the translation of smg mRNA. We have also analyzed in detail the very early developmental arrest associated with wisp mutations. Pronuclear migration does not occur in activated eggs laid by wisp mutant females. Finally, we find that WISP function is also needed during oogenesis to regulate the poly(A) tail length of dmos during oocyte maturation and to maintain a high level of active (phospho-) mitogen-activated protein kinases (MAPKs).
- Subjects :
- Amino Acid Sequence
Animals
Drosophila Proteins biosynthesis
Drosophila Proteins chemistry
Drosophila Proteins genetics
Drosophila melanogaster embryology
Embryo, Nonmammalian metabolism
Enzyme Activation
Female
Male
Meiosis
Mitogen-Activated Protein Kinases metabolism
Molecular Sequence Data
Mutation genetics
Poly A metabolism
Polynucleotide Adenylyltransferase genetics
Protein Binding
Protein Biosynthesis
RNA-Binding Proteins biosynthesis
RNA-Binding Proteins metabolism
Repressor Proteins biosynthesis
Drosophila Proteins metabolism
Drosophila melanogaster cytology
Drosophila melanogaster enzymology
Oocytes enzymology
Oogenesis
Polynucleotide Adenylyltransferase chemistry
Polynucleotide Adenylyltransferase metabolism
Sequence Homology, Amino Acid
Subjects
Details
- Language :
- English
- ISSN :
- 0016-6731
- Volume :
- 178
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Genetics
- Publication Type :
- Academic Journal
- Accession number :
- 18430932
- Full Text :
- https://doi.org/10.1534/genetics.107.084558