NORMAL GENOMIC

• Davis T, Kurihara J, Yoshino E, Yamamoto D
• Genomic organisation of the neural sex determination gene fruitless (fru) in the Hawaiian species Drosophila silvestris and the conservation of the fru BTB protein-protein-binding domain throughout evolution.
• Hereditas. 2000; 132: 67-78
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• We report the cloning and sequencing of the fru gene from the Hawaiian picture-wing species Drosophila silvestris. The fru gene has seven exons spanning 15-kb encoding two transcripts with ORFs of 841 and 695 amino acids. The protein encoded by the fruA transcript is well conserved with the D. melanogaster type A protein, particularly the BTB protein-protein-binding domain, which is encoded by exons I and II and is 100% conserved. The peptide encoded by exon III has several sequence differences but these are confined mostly to regions of repetitive sequence and exons IV to VI are well conserved. The peptide encoded by exon VII is semi-conserved for the 5' end and 100% conserved for the Zinc finger domains; the rest of the peptide is virtually unconserved. The FRUA protein has a BTB domain and two zinc finger domains whereas the FRUC protein only has the BTB domain. The genomic DNA sequence encoding the BTB domain of the fru gene has been cloned from 21 species of Diptera. The protein-coding sequence is highly conserved and the amino acid sequence is identical except for two changes in the Tephritidae. The intron sequences are completely unconserved except between very closely related species such as the Hawaiian Drosophila. The phylogeny produced using the BTB exon sequences suggests that the most closely related mainland Drosophila species to the Hawaiian clade is D. moriwakii of the melanica species group. The phylogeny also shows that the Scaptomyza are closely related to the Hawaiian Drosophila so supporting a Hawaiian origin for the Scaptomyza. The genus Zaprionus is placed in the subgenus Drosophila closely related to D. immigrans along with the genera Samoaia and Liodrosophila.

• Mazroui R, Puoti A, Kramer A
• Splicing factor SF1 from Drosophila and Caenorhabditis: presence of an N-terminal RS domain and requirement for viability.
• RNA. 1999; 5: 1615-31
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• Splicing factor SF1 contributes to the recognition of the 3' splice site by interacting with U2AF65 and binding to the intron branch site during the formation of the early splicing complex E. These interactions and the essential functional domains of SF1 are highly conserved in Saccharomyces cerevisiae. We have isolated cDNAs encoding SF1 from Drosophila (Dm) and Caenorhabditis (Ce). The encoded proteins share the U2AF65 interaction domain, a hnRNP K homology domain, and one or two zinc knuckles required for RNA binding as well as Pro-rich C-terminal sequences with their yeast and mammalian counterparts. In contrast to SF1 in other species, DmSF1 and CeSF1 are characterized by an N-terminal region enriched in Ser, Arg, Lys, and Asp residues with homology to the RS domains of several splicing proteins. These domains mediate protein-protein or protein-RNA interactions, suggesting an additional role for DmSF1 and CeSF1 in pre-mRNA splicing. Human (Hs), fly, and worm SF1 interact equally well with HsU2AF65 or the Drosophila homolog DmU2AF50. Moreover, DmSF1 lacking its N terminus is functional in prespliceosome formation in a HeLa splicing system, emphasizing the conserved nature of interactions at an early step in spliceosome assembly. The Ce-SF1 gene is located in a polycistronic transcription unit downstream of the genes encoding U2AF35 (uaf-2) and a cyclophilin (cyp-13), implying the coordinate transcriptional regulation of these genes. Injection of double-stranded RNA into C. elegans results in embryonic lethality; thus, the SF1 gene is essential not only in yeast but also in at least one metazoan.