Abstract
The Drosophila melanogaster ovarian tumor (otu) gene encodes two novel protein isoforms that are required at multiple stages of oogenesis. We have examined the activity of a set of C-terminal truncation Otu proteins as well as a GFP-tagged Otu (Otu-GFP). These experiments have shown that a putative Tudor domain in the central region of the large Otu isoform and a separate domain in the C-terminal region are required for regulation of cyst formation and oocyte maturation, respectively. We also present evidence that a portion of Otu co-fractionates with mRNA/protein complexes (mRNPs) and show that Otu-GFP associates with cytoplasmic aggregates at periphery of the nucleus at an intermediate stage of oogenesis. This study substantially clarifies the relationship between Otu structure and function and reveals new clues about interacting components.
