Abstract
Reaper, Hid, and Grim are three Drosophila cell death activators that each contain a conserved NH(2)-terminal Reaper, Hid, Grim (RHG) motif. We have analyzed the importance of the RHG motifs in Reaper and Grim for their different abilities to activate cell death during development. Analysis of chimeric R/Grim and G/Reaper proteins indicated that the Reaper and Grim RHG motifs are functionally distinct and help to determine specific cell death activation properties. A truncated GrimC protein lacking the RHG motif retained an ability to induce cell death, and unlike Grim, R/Grim, or G/Reaper, its actions were not efficiently blocked by the cell death inhibitors, Diap1, Diap2, p35, or a dominant/negative Dronc caspase. Finally, we identified a second region of sequence similarity in Reaper, Hid, and Grim, that may be important for shared RHG motif-independent activities.
Publication types
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Amino Acid Motifs
-
Amino Acid Sequence
-
Animals
-
Bacterial Outer Membrane Proteins / metabolism
-
Caspases / metabolism
-
Cell Death
-
Central Nervous System / embryology
-
Drosophila
-
Drosophila Proteins*
-
Genes, Dominant
-
Immunohistochemistry
-
Inhibitor of Apoptosis Proteins
-
Insect Proteins / metabolism
-
Lipoproteins / metabolism
-
Molecular Sequence Data
-
Neuropeptides / chemistry*
-
Neuropeptides / metabolism
-
Neuropeptides / physiology
-
Peptides / chemistry*
-
Peptides / metabolism
-
Peptides / physiology
-
Phenotype
-
Photoreceptor Cells, Invertebrate / metabolism
-
Recombinant Fusion Proteins / chemistry
-
Sequence Homology, Amino Acid
Substances
-
Bacterial Outer Membrane Proteins
-
DIAP1 protein, Drosophila
-
DIAP2 protein, Drosophila
-
Drosophila Proteins
-
HID protein, Drosophila
-
Inhibitor of Apoptosis Proteins
-
Insect Proteins
-
Lipoproteins
-
Neuropeptides
-
Peptides
-
Recombinant Fusion Proteins
-
grim protein, Drosophila
-
rpr protein, Drosophila
-
Caspases
-
dronc protein, Drosophila