The Drosophila retained/dead ringer gene and ARID gene family function during development.
The recently discovered ARID family of proteins interact with DNA through a phylogenetically conserved sequence termed the A/T Interaction Domain (ARID). The retained/dead ringer (retn/dri) gene of Drosophila melanogaster is a founding member of the ARID gene family, and of the eARID subfamily. This subfamily exhibits an extended region of sequence similarity beyond the core ARID motif and a separate conserved domain termed the REKLES domain. retn/dri is involved in a range of developmental processes, including axis patterning and muscle development. The retn/dri ARID motif has been shown by in vitro studies to exhibit sequence-specific DNA binding activity. Here we demonstrate that the ARID domain is essential for the in vivo function of retn/dri during embryonic development by showing that a mutant form of RETN/DRI, deleted for part of the ARID domain and unable to bind DNA in vitro, cannot rescue the retn/dri mutant phenotype. In the presence of wild-type RETN/DRI this construct acts as a dominant negative, providing additional support for the proposal that RETN/DRI acts in a multiprotein complex. In contrast, we are yet to find an in vivo role for the REKLES domain, despite its clear evolutionary conservation. Finally, we have used germline clone analysis to reveal a requirement for retn/dri in the Drosophila preblastoderm syncytial mitoses.
Shandala
Tetyana
T
Centre for the Molecular Genetics of Development and Dept of Molecular Biosciences, Adelaide University, SA, Australia.
Kortschak
R Daniel
RD
Saint
Robert
R
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D002453:Cell Cycle; D002455:Cell Division; D004247:DNA / Q000378:metabolism; D004330:Drosophila; D029721:Drosophila Proteins; D017353:Gene Deletion; D018507:Gene Expression Regulation, Developmental; D005799:Genes, Dominant; D018398:Homeodomain Proteins / Q000235:genetics* / Q000502:physiology*; D006801:Humans; D007150:Immunohistochemistry; D008856:Microscopy, Fluorescence; D008938:Mitosis; D008969:Molecular Sequence Data; D009154:Mutation; D009687:Nuclear Proteins / Q000235:genetics* / Q000502:physiology*; D010641:Phenotype; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid
D029721:Drosophila Proteins; D018398:Homeodomain Proteins; D009687:Nuclear Proteins; C098342:Retn protein, Drosophila; D004247:DNA