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The RNA-binding protein Tsunagi interact ... RNA during Drosophila oogenesis
The RNA-binding protein Tsunagi interacts with Mago Nashi to establish polarity and localize oskar mRNA during Drosophila oogenesis.
3
In Drosophila melanogaster, formation of the axes and the primordial germ cells is regulated by interactions between the germ line-derived oocyte and the surrounding somatic follicle cells. This reciprocal signaling results in the asymmetric localization of mRNAs and proteins critical for these oogenic processes. Mago Nashi protein interprets the posterior follicle cell-to-oocyte signal to establish the major axes and to determine the fate of the primordial germ cells. Using the yeast two-hybrid system we have identified an RNA-binding protein, Tsunagi, that interacts with Mago Nashi protein. The proteins coimmunoprecipitate and colocalize, indicating that they form a complex in vivo. Immunolocalization reveals that Tsunagi protein is localized within the posterior oocyte cytoplasm during stages 1-5 and 8-9, and that this localization is dependent on wild-type mago nashi function. When tsunagi function is removed from the germ line, egg chambers develop in which the oocyte nucleus fails to migrate, oskar mRNA is not localized within the posterior pole, and dorsal-ventral pattern abnormalities are observed. These results show that a Mago Nashi-Tsunagi protein complex is required for interpreting the posterior follicle cell-to-oocyte signal to define the major body axes and to localize components necessary for determination of the primordial germ cells.
Mohr SE, Dillon ST, Boswell RE
Genes & development
2001-11-01 00:00
15
21
2886-99
Alleles,Amino Acid Sequence,Animals,Base Sequence,Cell Lineage,DNA Mutational Analysis,DNA, Complementary,Drosophila Proteins,Drosophila melanogaster,Electrophoresis, Polyacrylamide Gel,Female,Gene Expression Regulation, Developmental,Germ Cells,In Situ Hybridization,Insect Proteins,Male,Molecular Sequence Data,Nuclear Proteins,Oocytes,Precipitin Tests,Protein Binding,RNA, Messenger,RNA-Binding Proteins,Sequence Homology, Amino Acid,Time Factors,Transgenes,Two-Hybrid System Techniques,DNA, Complementary,Drosophila Proteins,Insect Proteins,Mago protein, Drosophila,Nuclear Proteins,RNA, Messenger,RNA-Binding Proteins,oskar protein, Drosophila,tsunagi protein, Drosophila
Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, Colorado 80309-0347, USA
Genes Dev.
NIGMS GM07135, NIGMS GM17954, NIGMS GM57989
0890-9369
10.1101/gad.927001
111
True
11691839
