Segmental Polarity in Drosophila melanogaster: Genetic Dissection of fused in a Suppressor of fused Background Reveals Interaction With costal-2

• Published in: Genetics (Austin) 1993-12, Vol.135 (4), p.1047-1062
• Main Authors: Preat, T, Therond, P, Limbourg-Bouchon, B, Pham, A, Tricoire, H, Busson, D, Lamour-Isnard, C
• Format: Article
• Language: English
• Subjects: Alleles; Amino Acid Sequence; Animals; Base Sequence; Biological and medical sciences; Classical genetics, quantitative genetics, hybrids; DNA; DNA Primers; Drosophila melanogaster; Drosophila melanogaster - embryology; Drosophila melanogaster - genetics; Drosophila Proteins; Female; Fundamental and applied biological sciences. Psychology; Gene Expression; Genes; Genes, Recessive; Genetics; Genetics of eukaryotes. Biological and molecular evolution; Insects; Invertebrata; Investigations; Male; Molecular Sequence Data; Phenotype; Protein-Serine-Threonine Kinases - genetics; Protein-Serine-Threonine Kinases - metabolism; Suppression, Genetic
• ISSN: 0016-6731; 1943-2631; 1943-2631
• DOI: 10.1093/genetics/135.4.1047

fused (fu) is a segment polarity gene that encodes a putative serine/threonine kinase. A complete suppressor of the embryonic and adult phenotypes of fu mutants, Suppressor of fused (Su(fu)), was previously described. The amorphic Su(fu) mutation is viable and displays no phenotype by itself. We have used this suppressor as a tool to perform a genetic dissection of the fu gene. Analysis of the interaction between Su(fu) and 33 fu alleles shows that they belong to three different classes. Defects due to class I fu alleles are fully suppressed by Su(fu). Class II fu alleles lead to a new segment polarity phenotype in interaction with Su(fu). This phenotype corresponds to embryonic and adult anomalies similar to those displayed by the segment polarity mutant costal-2 (cos-2). Class II alleles are recessive to class I alleles in a fu[I]/fu[II];Su(fu)/Su(fu) combination. Class 0 alleles, like class I alleles, confer a normal segmentation phenotype in interaction with Su(fu). However class II alleles are dominant over class 0 alleles in a fu[0]/fu[II];Su(fu)/Su(fu) combination. Alleles of class I and II correspond to small molecular events, which may leave part of the Fu protein intact. On the contrary, class 0 alleles correspond to large deletions. Several class I and class II fu mutations have been mapped, and three mutant alleles were sequenced. These data suggest that class I mutations affect the catalytic domain of the putative Fu kinase and leave the carboxy terminal domain intact, whereas predicted class II proteins have an abnormal carboxy terminal domain. Su(fu) enhances the cos-2 phenotype and cos-2 mutations interact with fu in a way similar to Su(fu). All together these results suggest that a close relationship might exist between fu, Su(fu) and cos-2 throughout development. We thus propose a model where the Fu+ kinase is a posterior inhibitor of Costal-2+ while Su(fu)+ is an activator of Costal-2+. The expression pattern of wingless and engrailed in fu and fu;Su(fu) embryos is in accordance with this interpretation.