dodo


DEVELOPMENTAL BIOLOGY

Effects of Mutation or Deletion

The dodo mutant resembles Egfr- and hs-CF2. dodo was originally identified by genomic sequencing and transcript mapping (Maleszka, 1996). To reveal phenotypes associated with loss-of-function mutations without preset screening criteria, small overlapping chromosomal deletions were generated (Maleszka, 1996) that uncovered the entire dodo transcription unit in addition to two flanking genes: penguin (pen) and fli-I. The dodo-null genotype was confirmed by Northern blot analysis. The trans-heterozygous deletion mutant is lethal but viability can be restored by replacing the genomic copy of fli-I with a transgene (Maleszka, 1996). The resulting trans-heterozygotes lacking both the dodo and pen transcription units are viable and the surviving adult females permit the examination of possible oogenic phenotypes, particularly those associated with the MAPK signaling defects in the follicle cells. Initial examination showed a ventralized eggshell phenotype that was consistent but of low penetrance (35% at 25°C), ranging in expressivity from fused dorsal appendages to no appendages at all. Because the deletion mutant (in the background of the fli-I transgene) is also null for the gene pen, it was necessary to determine whether or not the ventralized phenotype is the result of dodo deletion. To this end it was shown that the phenotype can be rescued almost completely by supplying an exogenous dodo transgene under the transcriptional control of a heat-shock promoter in a dose-dependent manner (Hsu, 2001).


REFERENCES

Arevalo-Rodriguez, M., et al. (2000). Cyclophilin A and Ess1 interact with and regulate silencing by the Sin3-Rpd3 histone deacetylase. EMBO J. 19(14): 3739-49. 10899127

Crenshaw, D. G., et al. (1998). The mitotic peptidyl-prolyl isomerase, Pin1, interacts with Cdc25 and Plx1. EMBO J. 17(5): 1315-27. 9482729

Fujimori, F., et al. (1999). Mice lacking Pin1 develop normally, but are defective in entering cell cycle from G(0) arrest. Biochem. Biophys. Res. Commun. 265: 658-663. 10600477

Hanes, S. D., Shank, P. R. and Bostian, K. A. (1989). Sequence and mutational analysis of ESS1, a gene essential for growth in Saccharomyces cerevisiae. Yeast 5(1): 55-72. 2648698

Hani, J., Stumpf, G. and Domdey, H. (1995). PTF1 encodes an essential protein in Saccharomyces cerevisiae, which shows strong homology with a new putative family of PPIases. FEBS Lett. 365(2-3): 198-202. 7781779

Hani, J., et al. (1999). Mutations in a peptidylprolyl-cis/trans-isomerase gene lead to a defect in 3'-end formation of a pre-mRNA in Saccharomyces cerevisiae. J. Biol. Chem. 274(1): 108-16. 9867817

Hsu, T., et al. (1996). The transcription factor CF2 is a mediator of Egfr -activated dorsoventral patterning in Drosophila oogenesis. Genes Dev. 10: 1411-1421. 8647437

Hsu, T., McRackan, D., Vincent, T. S. and de Couet, H. G. (2001). Drosophila Pin1 prolyl isomerase Dodo is a MAP kinase signal responder during oogenesis. Nature Cell Biol. 3: 538-543. 11389437

Lu, K. P., Hanes, S. D. and Hunter, T. (1996). A human peptidyl-prolyl isomerase essential for regulation of mitosis. Nature 380(6574): 544-7. 8606777

Maleszka, R., et al. (1996). The Drosophila melanogaster dodo (dod) gene, conserved in humans, is functionally interchangeable with the ESS1 cell division gene of Saccharomyces cerevisiae. Proc. Natl Acad. Sci. 93: 447-451. 8552658

Mantrova, E. Yu. and Hsu, T. (1998). Down-regulation of transcription factor CF2 by the Drosophila Ras/MAP kinase signaling in oogenesis: cytoplasmic retention and degradation. Genes Dev. 12: 1166-1175. 9553046

Morris, D. P., Phatnani, H. P. and Greenleaf, A. L. (1999). Phospho-carboxyl-terminal domain binding and the role of a prolyl isomerase in pre-mRNA 3'-end formation. J. Biol. Chem. 274(44): 31583-7. 10531363

Ranganathan, R., et al. (1997). Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent. Cell 89(6): 875-86. 9200606

Shen, M., et al. (1998). The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins. Genes Dev. 12(5): 706-20. 9499405

Wu, X., et al. (2000). The Ess1 prolyl isomerase is linked to chromatin remodeling complexes and the general transcription machinery. EMBO J. 19(14): 3727-38. 10899126

Zhou, X. Z., et al. (2000). Pin1-dependent prolyl isomerization regulates dephosphorylation of Cdc25C and tau proteins. Mol. Cell 6(4): 873-83. 11090625


dodo: Biological Overview | Evolutionary Homologs | Regulation | Developmental Biology | Effects of Mutation

date revised: 30 June 2001

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