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[Molecular mechanisms of development and differentiation of eye structures in Drosophila and vertebrates].

The development of the eye is compared in Drosophila and vertebrates. Although the structure of the compound eye of invertebrates and of the cameral eye of vertebrates differs morphologically, there are striking similarities at the molecular level. Three groups of genes control morphogenesis of the eye: the genes responsible for eye rudiment formation, neurogenic genes, and proneural genes. In the eye rudiments of Drosophila and vertebrates, the homologous regulatory homeobox-containing genes ey/Pax6, so/Six3, rx/Rx, and optix/Optx2 are expressed. Transcription factors encoded by these conservative genes are involved in specific interactions with DNA. Another set of homologous genes, eya/Eya and dac/DACH/Dac, is also expressed during this developmental period. These genes encode nuclear transcription factors that are devoid of DNA-binding domains but are involved in the protein-protein interactions that control gene expression. Transcriptional complexes, which are products of homeobox-containing genes and nuclear factors, control morphogenesis of the eye in Drosophila and vertebrates. A similar set of homologous regulatory and nuclear genes controls morphogenesis during formation of ectopic eyes in Drosophila and vertebrates. Molecular biology approaches have allowed eye development to be examined at the level of developmental mechanisms. It has become evident that progress in understanding the mechanisms of eye development is due to studies carried out on Drosophila. Supporters of the idea of the polyphyletic origin of the compound and cameral eyes have noted significant differences in their structure and have failed to find distinct common features in their development. The hypothesis of the monophyletic origin of eyes has been substantiated by the results of molecular investigations.

Animals↗
PubMed1992

Molecular cloning and characterization of the inositol 1,4,5-trisphosphate receptor in Drosophila melanogaster.

We isolated a cDNA encoding an inositol 1,4,5-trisphosphate receptor (InsP3R) of Drosophila melanogaster. The predicted Drosophila InsP3R (2,833 amino acids) has extensive sequence similarity to the mouse InsP3R. The polypeptide encoded by the cDNA was functionally expressed and showed characteristic InsP3-binding activity. The Drosophila InsP3R gene is located at the region 83A5-9 on the third chromosome and expresses throughout development but predominantly in the adult. Localization of the InsP3R mRNA in adult tissues suggests strong expression in the retina and antenna, indicating the involvement of the InsP3R in visual and olfactory transduction. In addition, the InsP3R mRNA is abundant in the legs and thorax, which are enriched with a muscular system. Such localization is apparently consistent with the quantitatively predominant sites for [3H]InsP3 binding in Drosophila and the fleshfly (Boettcherisca peregrina). The present study points to the likely functional importance of the InsP3/Ca2+ signaling system in Drosophila.

Amino Acid Sequence↗
PubMed1992

A single locus encodes both phenylalanine hydroxylase and tryptophan hydroxylase activities in Drosophila.

We have used a full-length clone encoding rabbit tryptophan hydroxylase (TRH) to isolate the Drosophila homologue (DTPH). Southern analysis of Drosophila genomic DNA reveals a pattern indicative of a single gene. The single transcript is expressed in adult head and body mRNA but is also detected in mRNA from early embryos. The embryonic transcript is ubiquitously expressed and appears to concentrate in yolk granules. In situ hybridization of TRH-homologous antisense RNA probe to sectioned tissue from third instar larvae demonstrated the presence of this transcript in fat body and cuticular tissue. Developmental immunoblot analysis using antibodies raised against a beta-galactosidase-Drosophila fusion protein revealed a 45-kDa embryonic protein also detected in female abdomens and a 50-kDa protein found in larval and adult stages. Immunocytochemical analysis of the Drosophila protein in the larval central nervous system showed that it appeared to be present in both serotonin- and catecholamine-containing neurons. A nonfusion protein generated in Escherichia coli hydroxylates both tryptophan and phenylalanine. We propose that there are only two aromatic amino acid hydroxylase genes in Drosophila: one encoding tyrosine hydroxylase, DTH, and DTPH, a gene encoding both tryptophan and phenylalanine hydroxylase activities.

Amino Acid Sequence↗
PubMed1992

The Drosophila G protein gamma subunit gene (D-G gamma 1) produces three developmentally regulated transcripts and is predominantly expressed in the central nervous system.

A genomic clone, 536, located at the 44CD region of polytene chromosomes of Drosophila melanogaster, has been characterized for its neurobiological importance. We found that this clone contains a gene which produces 2.6-, 1.3- and 1.1-kilobase (kb) RNAs. While the 2.6-kb RNA is expressed only in the head, the 1.3-kb RNA is present exclusively in the body. The 1.1-kb RNA, however, is found in both the head and body, but in much higher concentration in the head. DNA sequence analysis of a 2.6-kb RNA-specific cDNA showed that this gene encodes a 70-amino acid polypeptide which is the putative Drosophila homologue to the gamma subunit of the bovine G-protein. The Drosophila protein, named D-G gamma 1, shares 46, 43, and 28% identity, and 59, 52, and 60% similarity, with the gamma 2, gamma 3, and gamma t proteins of bovine G proteins, respectively. Sequencing of the 1.1-kb RNA-specific cDNA clone revealed that the 1.1-kb RNA is produced from the 2.6-kb transcription unit by usage of an alternative polyadenylation site, and has a coding region identical to that of the 2.6-kb RNA. Genomic Southern blot hybridization indicated that the Drosophila genome has only one D-G gamma 1 gene. Throughout development the 1.1-kb RNA is found to be the most prevalent species; its level peaks between 9 and 12 h of embryogenesis. As is the case for the other G protein genes of Drosophila, the D-G gamma 1 gene is predominantly expressed in the central nervous system of the fly.

Amino Acid Sequence↗
PubMed2005

Drosophila melanogaster: a model for the study of DNA damage checkpoint response.

The cells of metazoans respond to DNA damage by either arresting their cell cycle in order to repair the DNA, or by undergoing apoptosis. This response is highly conserved across species, and many of the genes involved in this DNA damage response have been shown to be inactivated in human cancers. This suggests the importance of DNA damage response with regard to the prevention of cancer. The DNA damage checkpoint responses vary greatly depending on the developmental context, cell type, gene expression profile, and the degree and nature of the DNA lesions. More valuable information can be obtained from studies utilizing whole organisms in which the molecular basis of development has been well established, such as Drosophila. Since the discovery of the Drosophila p53 orthologue, various aspects of DNA damage responses have been studied in Drosophila. In this review, I will summarize the current knowledge on the DNA damage checkpoint response in Drosophila. With the ease of genetic, cellular, and cytological approaches, Drosophila will become an increasingly valuable model organism for the study of mechanisms inherent to cancer formation associated with defects in the DNA damage pathway.

Animals↗
PubMed1991

Structural and functional conservation of synaptotagmin (p65) in Drosophila and humans.

Synaptotagmin (p65) is an abundant synaptic vesicle protein that contains two copies of a sequence that is homologous to the regulatory region of protein kinase C. Full length cDNAs encoding human and Drosophila synaptotagmins were characterized to study its structural and functional conservation in evolution. The deduced amino acid sequences for human and rat synaptotagmins show 97% identity, whereas Drosophila and rat synaptotagmins are only 57% identical but exhibit a selective conservation of the two internal repeats that are homologous to the regulatory region of protein kinase C (78% invariant residues in all three species). The two internal repeats of synaptotagmin are only slightly more homologous to each other than to protein kinase C, and the differences between the repeats are conserved in evolution, suggesting that they might not be functionally equivalent. The cytoplasmic domains of human and Drosophila synaptotagmins produced as recombinant proteins in Escherichia coli specifically bound phosphatidylserine similar to rat synaptotagmin. They also hemagglutinated trypsinized erythrocytes at nanomolar concentrations. Hemagglutination was inhibited both by negatively charged phospholipids and by a recombinant fragment from rat synaptotagmin that contained only a single copy of the two internal repeats. Together these results demonstrate that synaptotagmin is highly conserved in evolution compatible with a function in the trafficking of synaptic vesicles at the active zone. The similarity of the phospholipid binding properties of the cytoplasmic domains of rat, human, and Drosophila synaptotagmins and the selective conservation of the sequences that are homologous to protein kinase C suggest that these are instrumental in phospholipid binding. The human gene for synaptotagmin was mapped by Southern blot analysis of DNA from somatic cell hybrids to chromosome 12 region cen-q21, and the Drosophila gene by in situ hybridization to 23B.

Amino Acid Sequence↗
PubMed1991

Analysis of the molecular mechanisms for the species-specific transcription of Drosophila and human tRNA gene transcription components.

The transcription of eucaryotic tRNA genes requires two factors IIIB and IIIC, in addition to RNA polymerase III, to reconstitute this process in vitro. We have examined the functional exchangeability of these components from Drosophila and human systems. The reconstitution of heterologous IIIB and IIIC components demonstrated that neither factor will functionally substitute for the homologous components to activate tRNA gene transcription. The addition of the heterologous Drosophila factors to HeLa transcription assays causes an inhibition of RNA synthesis that is dependent upon the order of addition of these proteins to the DNA template. Thus, it appears that tRNA gene transcription in these systems is species-specific. We have further analyzed the reason for the apparent incompatibilities of these components by the use of stable complex formation assays. We find that human HeLa IIIB and Drosophila IIIC are unable to form stably associated complexes with a tRNA gene template, whereas the Drosophila IIIB and HeLa IIIC do form stable but nonproductive complexes. These results demonstrate that specific IIIC-IIIB interactions are critical in the formation of productive transcription complexes and are responsible for the observed species specificity of Drosophila and human tRNA gene transcription.

Animals↗
PubMed1991

Queuine metabolism and cadmium toxicity in Drosophila melanogaster.

Queuine can replace guanine in the anticodon of certain tRNAs and is a hypermodified guanine derivative that can be synthesized by bacteria but not by mice. The study demonstrates that Drosophila can incorporate dietary queuine into tRNA but cannot synthesize it de novo for this purpose. Since an earlier study had shown that dietary CdCl2 caused Drosophila to increase greatly the proportion of queuine-containing tRNA over non-queuine tRNA the ability of dietary queuine to counteract cadmium toxicity was evaluated. When queuine was present in the cadmium-containing medium more pupae matured into adults than when queuine was absent. Other studies had demonstrated that the transglycosylase enzyme, that catalyzes the replacement of guanine in the anticodon of tRNA by queuine, is present in Drosophila larvae but the tRNA is virtually devoid of queuine. This study shows that in the presence of dietary queuine the larval tRNA contains abundant amounts of queuine. Therefore, we postulate a significant role for bacteria in supplying queuine to Drosophila for its incorporation into tRNA and that the control of this process by Drosophila is passive, i.e. is not an essential feature in differentiation.

Animals↗
PubMed1990

P-element-mediated enhancer detection allows rapid identification of developmentally regulated genes and cell specific markers in Drosophila.

We have employed a new technique in Drosophila that allows in vivo detection of genomic regulatory elements using a beta-galactosidase reporter gene. A translational fusion of the reporter gene to the P-transposase gene, which is encoded by the P-transposon of Drosophila, places the expression of beta-galactosidase under the control of the weak P-transposase promoter. Flies carrying single insertions of this P-element construct at different locations in the Drosophila genome frequently stain for beta-galactosidase activity in a temporally and spatially restricted fashion in embryos, larvae and adult ovaries, reflecting the influence of nearby genomic regulatory elements on the P-transposase promoter. This technique is a powerful tool as it can be used to produce very many different cell markers and to isolate developmentally regulated genes in Drosophila. We discuss the implications of our results and the applications of the technique to further the study of Drosophila development.

Animals↗
PubMed1988

Ionic currents of Drosophila neurons in embryonic cultures.

Drosophila offers a unique opportunity to determine how the genome codes for ionic channels in an organized nervous system. Considerable progress has already been made in studying the molecular biology of Drosophila K channels. In order for similar progress to be made on neuronal voltage-dependent Ca channels, a physiological preparation is needed in which the function of these channels can be directly studied. The patch-clamp studies reported here show that cultures of embryonic Drosophila cells (Seecof and Unanue, 1968) meet this need. These cultures provide the first opportunity to study with voltage-clamp techniques the Ca and Na currents of Drosophila neurons. The focus of these studies is on the Ca current; however, descriptions of the K and Na currents are also given since they help to characterize the cells studied and the quality of the voltage clamp. The voltage-dependent K, Na, and Ca currents of Drosophila neurons are very similar to those of molluscan neurons and other better studied neurons. The K currents are the largest currents in these neurons, averaging over 300 pA at +20 mV. There are 2 classes of Ca-independent K currents, inactivating currents that are 4-AP sensitive, and noninactivating currents that are insensitive to 4-AP. A large fraction of the K currents are located in the somal membrane. The Na currents are TTX sensitive and probably located in the processes. The peak amplitudes of the Ca currents vary from 0 to over 100 pA in these neurons, averaging 40 pA. With 5 mM external Ca2+ or Ba2+, the Ba currents are about twice as large as the Ca currents. Although 100 microM Cd2+ completely blocks the Ca current, organic blockers have very little effect. Variable inactivation characteristics and sensitivity to washout suggest the possibility of multiple types of Ca channels. A search for single-channel Ba currents in the somal membrane was unsuccessful.

Animals↗
PubMed1989

Immunological and molecular characterization of Go alpha-like proteins in the Drosophila central nervous system.

The alpha subunits of heterotrimeric G proteins are responsible for the coupling of receptors for a wide variety of stimuli to a number of intracellular effector systems. In the nervous system of vertebrates, high levels of a specific class of G protein (Go alpha) are expressed. The alpha subunit of Go serves as a substrate for modification by pertussis toxin (PTX). In this report, we demonstrate that the Drosophila heads contain high levels of a 40-kDa PTX substrate. Modification of this protein by PTX is modulated in a manner similar to that observed for vertebrate G proteins. The PTX substrate in Drosophila is also recognized specifically by antibodies raised against peptide sequences found specifically in vertebrate Go alpha. Vertebrate Go alpha probes were used to identify a Drosophila cDNA coding for a potential PTX substrate with high sequence identity (82%) to vertebrate Go alpha. An additional cDNA coding for a related Go alpha has also been isolated. The two cDNAs differ only in the 5'-untranslated and amino-terminal regions of the protein. This observation, in addition to Northern analysis, suggests that alternate splicing may generate a variety of Go alpha-like proteins in Drosophila. In situ hybridization of specific probes to tissue sections indicates that the mRNAs coding for Go alpha-like proteins in Drosophila are expressed primarily in neuronal cell bodies and, at lower levels, in the eyes.

Adenosine Diphosphate Ribose↗
PubMed1985

Glyceraldehyde-3-phosphate dehydrogenase from Drosophila melanogaster. Identification of two isozymic forms encoded by separate genes.

The enzyme glyceraldehyde-3-phosphate dehydrogenase from Drosophila melanogaster has been purified, and these preparations contain two subunits forms which have molecular weights of 37,000 and 35,500, respectively. Each subunit is found in crude extracts, and two activity bands are seen in nondenaturing acrylamide gels. Translation of Drosophila poly(A)-containing RNA results in two products which are precipitable with anti-glyceraldehyde-3-phosphate dehydrogenase serum. Two recombinant DNA clones have been isolated from a genomic library of Drosophila DNA. Each of these clones has the ability to hybrid select mRNAs which translate into both subunit forms. These clones have been genetically characterized by in situ hybridization and restriction mapping. One clone hybridizes to region 13F and the other to region 43E of the Drosophila cytogenetic map. Therefore, it appears that the Drosophila melanogaster genome contains two unlinked genes for glyceraldehyde-3-phosphate dehydrogenase; one of them encodes a protein of 37,000 daltons, the other a protein of 35,500 daltons.

Animals↗
PubMed1986

DNA ligase from Drosophila melanogaster embryos. Purification and physical characterization.

A DNA ligase has been purified approximately 2,100-fold, to near-homogeneity, from Drosophila melanogaster 6-12-h embryos and was shown to catalyze the formation of 3',5'-phosphodiester bonds. Polypeptides with molecular weights 83,000, 75,000, and 64,000 were observed when the purified enzyme was electrophoresed under denaturing conditions. These polypeptides were shown by partial proteolysis studies and two-dimensional gel analysis to be structurally related. The two smaller polypeptides were presumably derived from the largest, 83,000 molecular weight protein, by proteolysis during purification or in vivo. All three polypeptides formed enzyme-adenylylate complexes in the absence of DNA. Drosophila DNA ligase had a Stokes radius of 45 A, a sedimentation coefficient of 4.3 S, and a frictional ratio of 1.6, yielding a calculated molecular weight of 79,800. These studies indicate that DNA ligase from Drosophila embryos is a monomer. The purified ligase was free of detectable ATPase, nuclease, topoisomerase, and DNA polymerase activities. The enzyme exhibited an absolute requirement for ATP in the joining reaction. A divalent metal was required and N-ethylmaleimide inhibited the reaction. Formation of phosphodiester bonds by Drosophila ligase required the presence of 5'-phosphoryl and 3'-hydroxyl termini. The purified enzyme restored biological activity to endonucleolytically cleaved pBR322 DNA. The specific activity of Drosophila DNA ligase was highest in unfertilized eggs. Developing embryos had 5-10-fold more ligase activity than at any later time in development.

Adenosine Triphosphate↗
PubMed1988

Drosophila basement membrane procollagen IV. I. Protein characterization and distribution.

A collagen was isolated from Drosophila E85, Schneider line 2L and Kc cell cultures. The purified protein was characterized and antibodies were raised against it. Immunofluorescence microscopy locates this material to the regions of basement membranes of Drosophila embryos, larvae, and adults. The molecules are mostly, or entirely, homotrimers of one polypeptide chain linked by interchain disulfide bonds. The partial amino acid sequences of a cyanogen bromide cleavage product of this chain are identical with a part of the virtual translation product of the Drosophila pro alpha 1(IV) nucleotide sequence that is reported in the accompanying paper. This gene is at Drosophila chromosome location 25C and was identified by the high homology of one part of it with the noncollagenous carboxyl terminus (NC1) of vertebrate type IV basement membrane collagens (Blumberg, B., MacKrell, A. J., Olson, P. F., Kurkinen, M., Monson, J. M., Natzle, J. E., and Fessler, J. H. (1987) J. Biol. Chem. 262, 5947-5950). In the electron microscope each molecule appears as a thread with a knob at one end, which contains the carboxyl peptide domains. The variation of flexibility of the thread was mapped along its length. Pulse-chase labeling of cell cultures showed that these molecules associate into disulfide-linked dimers and higher oligomers that can be partly separated by velocity sedimentation and are resolved by sodium dodecyl sulfate-agarose gel electrophoresis. Dimers and higher oligomers formed by overlap of the amino ends of molecules were found. Mild pepsin digestion of Drosophila embryos and larvae solubilized the corresponding disulfide-linked collagen molecules, and Staphylococcus aureus V8 protease peptide maps showed the identity of the collagen derived from animals and from cell cultures. Individual, native molecules have a sedimentation coefficient s20,w = 4.1 S, the dichroic spectrum and amino acid composition of a collagen, and a Tm = 31 degrees C. Positive in situ hybridization with a specific probe for this collagen began 6-8 h after egg laying and showed message in the locations of embryos and larvae which reacted with the antibodies. This included some prominent individual cells in the hemolymph.

Amino Acids↗
PubMed1983

Knotting of the circular duplex DNA by type II DNA topoisomerase from Drosophila melanogaster.

DNA molecules with topological knots can be detected in a reaction mixture of circular DNA and type II DNA topoisomerase purified from the embryos of Drosophila melanogaster. Similar to the DNA knotting reaction by bacteriophage T4-induced topoisomerase (Liu, L. F., Liu, C. C., and Alberts, B. M. (1980) Cell 19, 697-707), the knotting reaction by the Drosophila topoisomerase II requires a high ratio of enzyme/DNA. However, they differ in the following aspects: 1) the knotting reaction by the Drosophila enzyme is greatly stimulated by the presence of ATP; 2) the knotted DNA is a stable product in the reaction mixture over prolonged incubation; and 3) both the covalently closed circular DNA and its nicked form, which is devoid of any superhelical structure, can be knotted. The knotted DNA generated by the Drosophila topoisomerase II can be efficiently unknotted by a catalytic amount of Drosophila topoisomerase II, but not by topoisomerase I. The ionic strength optimum for the knotting reaction is close, but not identical, to the optimal condition for the unknotting and supercoil relaxation reactions. Aspects of DNA knotting are discussed.

Animals↗
PubMed1984

Similarities in structure and function of calf thymus and Drosophila casein kinase II.

Both calf and Drosophila contain a type II casein kinase with similar molecular structure and catalytic activity. Purified calf thymus casein kinase II is composed of three subunits of Mr = 44,000 (alpha), 40,000 (alpha'), and 26,000 (beta) (Dahmus, M.E. (1981) J. Biol. Chem. 256, 3319-3325), whereas the Drosophila enzyme is composed of two subunits of Mr = 36,700 (alpha) and 28,200 (beta) (Glover, C. V. C., Shelton, E. R., and Brutlag, D. L. (1983) J. Biol. Chem. 258, 3258-3265). The native form of the enzyme is an alpha 2 beta 2 tetramer. Polyclonal antibodies prepared against each enzyme react with both the alpha and beta subunits of the homologous enzyme and cross-react with both subunits of the heterologous enzyme. Reaction of polyclonal antibodies with proteins resolved by sodium dodecyl sulfate-polyacrylamide gel electrophoresis establishes that no significant difference in subunit molecular weight exists between the purified enzymes and the enzyme present in initial cell extracts. Each antibody effectively inhibits the in vitro activity of the homologous enzyme and causes a slight inhibition in the activity of the heterologous enzyme. Peptide maps derived from purified subunits indicate that the alpha and beta subunits are unique and that there is extensive primary sequence homology between the corresponding subunits of the calf and Drosophila enzyme. Casein kinase II from both sources phosphorylates the same subunits of calf thymus RNA polymerase II and an identical set of proteins in a complex mixture of acid-soluble proteins from Drosophila tissue culture cells. The striking similarity in molecular structure and catalytic activity between the calf and Drosophila enzyme suggests that casein kinase II has been highly conserved in evolution.

Animals↗
PubMed1993

Expression and nuclear translocation of the rel/NF-kappa B-related morphogen dorsal during the immune response of Drosophila.

The rel/NF-kappa B-related morphogen dorsal is a maternally expressed gene which is involved in the control of the dorso-ventral axis during early embryogenesis of Drosophila. We show that this gene is also expressed in the fat body of larvae and adults of Drosophila as well as in a tumorous blood cell line: its expression is noticeably enhanced upon bacterial (or lipopolysaccharide) challenge. This challenge also induces within 15-30 min a nuclear translocation of the dorsal protein. The genes encoding inducible antibacterial peptides in Drosophila contain kappa B-related nucleotide sequences and we show that the dorsal protein can bind to such motifs and sequence-specifically transactivate a reporter gene in co-transfection experiments with a Drosophila cell line. However, in dl1 mutants, in the absence of dorsal protein, the genes encoding antibacterial peptides retain their inducibility, suggesting a multifactorial control. The results indicate that in addition to its role in embryogenesis, dorsal is involved in the immune response of Drosophila. They also strengthen the analogy between the mammalian acute phase response and the insect immune response.

Animals↗
PubMed1997

Neuropeptide amidation in Drosophila: separate genes encode the two enzymes catalyzing amidation.

In vertebrates, the two-step peptide alpha-amidation reaction is catalyzed sequentially by two enzymatic activities contained within one bifunctional enzyme called PAM (peptidylglycine alpha-amidating mono-oxygenase). Drosophila head extracts contained both of these PAM-related enzyme activities: a mono-oxygenase (PHM) and a lyase (PAL). However, no bifunctional PAM protein was detected. We identified cDNAs encoding an active mono-oxygenase that is highly homologous to mammalian PHM. PHM-like immunoreactivity was found within diverse larval tissues, including the CNS, endocrine glands, and gut epithelium. Northern and Western blot analyses demonstrate RNA and protein species corresponding to the cloned PHM, but not to a bifunctional PAM, leading us to predict the existence of separate PHM and PAL genes in Drosophila. The Drosophila PHM gene displays an organization of exons that is highly similar to the PHM-encoding portion of the rat PAM gene. Genetic analysis was consistent with the prediction of separate PHM and PAL gene functions in Drosophila: a P element insertion line containing a transposon within the PHM transcription unit displayed strikingly lower PHM enzyme levels, whereas PAL levels were increased slightly. The lethal phenotype displayed by the dPHM P element insertion indicates a widespread essential function. Reversion analysis indicated that the lethality associated with the insertion chromosome likely is attributable to the P element insertion. These combined data indicate a fundamental evolutionary divergence in the genes coding for critical neurotransmitter biosynthetic enzymes: in Drosophila, the two enzyme activities of PAM are encoded by separate genes.

Amides↗