Simonetta Lisi a , Ilaria Mazzon a , and Kristin White a a Cutaneous Biology Research Center, Massachusetts General Hospital, Harvard Medical School, Charlestown, Massachusetts 02129 Corresponding author: Kristin White, CBRC, Massachusetts General Hospital, Bldg. 149, 13th St., Charlestown, MA 02129., firstname.lastname@example.org (E-mail) Communicating editor: T. S CH Ü PBACH Significant amounts of apoptosis take place during Drosophila development. The proapoptotic genes reaper ( rpr ), grim , and head involution defective ( hid ) are required for virtually all embryonic apoptosis. The proteins encoded by these genes share a short region of homology at their amino termini. The Drosophila IAP homolog THREAD/DIAP1 (TH/DIAP1), encoded by the thread ( th ) gene, negatively regulates apoptosis during development. It has been proposed that RPR, GRIM, and HID induce apoptosis by binding and inactivating TH/DIAP1. The region of homology between the three proapoptotic proteins has been proposed to bind to the conserved BIR2 domain of TH/DIAP1. Here, we present an analysis of loss-of-function and gain-of-function alleles of th , which indicates that additional domains of TH/DIAP1 are necessary for its ability to inhibit death induced by RPR, GRIM, and HID. In addition, that analysis of loss-of-function mutations demonstrates that th is necessary to block apoptosis very early in embryonic development. This may reflect a requirement to block maternally provided RPR and HID, or it may indicate another function of the TH/DIAP1 protein.
Genetics – Genetics Society of America
Published: Feb 1, 2000
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