Structure of a gene in the dipteran Chironomus tentans encoding a yeast ribosomal YL10 protein homologue.
Explore the source record for details and available documents.
Amino Acid Sequence↗
SEARCH · PubMed Health
Results for “Genes, Insect”
Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.
Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.
Infection rate of Aedes aegypti mosquitoes with dengue virus depends on the interaction between temperature and mosquito genotype.
Dengue fever is the most prevalent arthropod-transmitted viral disease worldwide, with endemic transmission restricted to tropical and subtropical regions of different temperature profiles. Temperature is epidemiologically relevant because it affects dengue infection rates in Aedes aegypti mosquitoes, the major vector of the dengue virus (DENV). Aedes aegypti populations are also known to vary in competence for different DENV genotypes. We assessed the effects of mosquito and virus genotype on DENV infection in the context of temperature by challenging Ae. aegypti from two locations in Vietnam, which differ in temperature regimes, with two isolates of DENV-2 collected from the same two localities, followed by incubation at 25, 27 or 32°C for 10 days. Genotyping of the mosquito populations and virus isolates confirmed that each group was genetically distinct. Extrinsic incubation temperature (EIT) and DENV-2 genotype had a direct effect on the infection rate, consistent with previous studies. However, our results show that the EIT impacts the infection rate differently in each mosquito population, indicating a genotype by environment interaction. These results suggest that the magnitude of DENV epidemics may not only depend on the virus and mosquito genotypes present, but also on how they interact with local temperature. This information should be considered when estimating vector competence of local and introduced mosquito populations during disease risk evaluation.
Aedes↗
deadpan, an essential pan-neural gene in Drosophila, encodes a helix-loop-helix protein similar to the hairy gene product.
Neural precursor cells in Drosophila acquire their identity early during their formation. In an attempt to determine whether all neural precursors share a set of genetic machinery, perhaps to control properties of differentiation common to all neurons, we used the enhancer-trap method to identify several genes (pan-neural genes) that are expressed in all neurons and/or their precursors. One of the pan-neural genes is deadpan, which encodes a helix-loop-helix protein closely related to the product of the segmentation gene hairy. The function of deadpan is essential for viability and is likely to be involved in the functional rather than the morphological differentiation of neurons.
Amino Acid Sequence↗
hu-li tai shao, a gene required for ring canal formation during Drosophila oogenesis, encodes a homolog of adducin.
Drosophila females bearing mutations in a previously undescribed gene, hu-li tai shao [(hts) too little nursing], produced egg chambers that contained fewer than the normal 15 nurse cells and that usually lacked an oocyte. The cytoplasmic bridges (ring canals) interconnecting nurse cells and the oocyte appeared abnormal, and lacked associated actin rings. The hts locus was found to encode a homolog of the mammalian membrane skeletal protein adducin. During oogenesis, hts mRNA became localized at the anterior of the oocyte and was subsequently expressed in a variety of embryonic tissues. These studies suggested that Drosophila adducin is needed to assemble actin at specialized regions of cell-cell contact in developing egg chambers and may also function at other times during the Drosophila life cycle.
Amino Acid Sequence↗
Spatial regulation of proneural gene activity: auto- and cross-activation of achaete is antagonized by extramacrochaetae.
The spatially restricted activities of achaete (ac) and scute (sc) are thought to define proneural clusters of potential sensory organ precursor cells in the imaginal discs of Drosophila. These genes encode transcriptional regulators of the basic helix-loop-helix (bHLH) class. We have found that direct, positive transcriptional autoregulation by the ac protein and cross-regulation by sc are essential for high-level expression of the ac promoter in the proneural cluster pattern and that autoactivation is important for the bristle-promoting function of the ac gene. These auto- and cross-regulatory activities are antagonized in a dose-dependent manner by the inhibitory HLH protein encoded by the extramacrochaetae (emc) gene. We have found that emc is expressed in the wing imaginal disc in a pattern strongly complementary to that of the proneural clusters. Our results indicate that emc plays an essential early role in defining territories of bristle-forming potential.
Animals↗
The Drosophila hedgehog gene is expressed specifically in posterior compartment cells and is a target of engrailed regulation.
cDNAs were isolated that represent transcripts of the Drosophila segment polarity gene, hedgehog (hh). Sequence analysis reveals a motif characteristic of a transmembrane domain, suggesting that the hh protein is membrane-associated. hh expression in epidermal cells is confined to the posterior compartments and coincides precisely with that of engrailed (en). Despite the similar patterns of expression in the cellular blastoderm, hh expression is independent of en, but hh expression becomes sensitive to and dependent on en during the extended germ band stage. The ectopic expression of hh that is normally induced in patched (ptc) mutant embryos does not appear in ptc en double mutants. We discuss these findings in terms of the relationship between en and hh, and the role of the hh function.
Amino Acid Sequence↗
AnoEST: toward A. gambiae functional genomics.
Here, we present an analysis of 215,634 EST and cDNA sequences of a major vector of human malaria Anopheles gambiae structured into the AnoEST database. The expressed sequences are grouped into clusters using genomic sequence as template and associated with inferred functional annotation, including the following: corresponding Ensembl gene prediction, putative orthologous genes in other species, homology to known proteins, protein domains, associated Gene Ontology terms, and corresponding classification into broad GO-slim functional groups. AnoEST is a vital resource for interpretation of expression profiles derived using recently developed A. gambiae cDNA microarrays. Using these cDNA microarrays, we have experimentally confirmed the expression of 7961 clusters during mosquito development. Of these, 3100 are not associated with currently predicted genes. Moreover, we found that clusters with confirmed expression are nonbiased with respect to the current gene annotation or homology to known proteins. Consequently, we expect that many as yet unconfirmed clusters are likely to be actual A. gambiae genes. [AnoEST is publicly available at http://komar.embl.de, and is also accessible as a Distributed Annotation Service (DAS).].
Animals↗
Structure and sequence of the Cu, Zn superoxide dismutase gene of Chymomyza amoena: phylogeny of the genus and codon-use evolution.
We have cloned and sequenced the Cu, Zn superoxide dismutase gene of Chymomyza amoena. The coding sequence has the same length as in Drosophila species and in Ceratitis capitata. There are two introns, located at the same sites as in Ceratitis. The second intron is absent in Drosophila: this places Chymomyza outside the Drosophila lineage, contrary to proposals based on anatomical and other evidence. The nucleotide or amino acid distances support a phylogeny in which Ceratitis first branches off the common stem, then Chymomyza splits before the divergence of the two major Drosophila subgenera. The estimated divergence times are 58 million for Chymomyza-Drosophila; 48 million years for the Drosophila subgenera. During the intervening 10 million years, the Drosophila lineage lost the second intron and evolved distinct codon-preferences: the G + C use in the third coding positions is increased by 69% in Drosophila relative to Chymomyza or Ceratitis.
Amino Acid Sequence↗
A muscle-specific actin gene from the Mediterranean fruit fly, Ceratitis capitata.
A characterization of an actin gene isolated from the genome of the Mediterranean fruit fly, Ceratitis capitata, including the complete sequencing of the coding, 3' and 5' flanking regions of this gene and a partial cDNA was carried out. The partial cDNA was derived from the 3' untranslated region of the actin gene described here, and has been used to identify this gene uniquely. The DNA sequence data presented here, together with the pattern of expression exhibited by this gene during development, strongly support the interpretation that this is a muscle-specific actin gene. Peaks of expression are seen in tissues and during temporal phases of development where muscle differentiation is occurring. The derived protein sequence of the Medfly acting gene shows the highest degrees of similarity, 98.4 and 96.6% respectively, with the two muscle-specific actin genes 79B and 88F from D. melanogaster. The Medfly actin gene also has a single intervening sequence, and an intron is found at the same position in the 79B and 88F actin genes. In the coding region at the DNA level, 17.2 and 16.4% nucleotide differences, respectively, are observed between the Medfly actin gene and these same two D. melanogaster actin genes. The disparity between the amino acid and nucleotide comparisons can be explained, in part, by a high level of synonymous changes in the DNA sequence. In addition, despite the many similarities, codon usage appears to be very different between the actin genes of these species.
Actins↗
Distribution of split 5.8S ribosomal RNA in Diptera.
Although the 5.8S ribosomal RNA (rRNA) of most eucaryotes consists of 155-170 nucleotides, in two dipterous species the 5.8S rRNA consists of two pieces, 123 and 30 nucleotides in length. The distribution of split 5.8S rRNA was studied in other Diptera and the most closely related order Siphonaptera to learn the origin of split 5.8S rRNA. Four species of mosquitoes, Culex tritaeniorhynchus, Culex pipiens molestus, Aedes albopictus, Anopheles sp. (Culicidae) had a single 5.8S rRNA consisting of approximately 154 nucleotides. A flea Ctenocephalides felis (Siphonaptera: Pulicidae) also had a single RNA of approximately 158 nucleotides. A crane fly (Tipulidae). a midge Orthocladius akamusi (Chironomidae), a robber fly (Asilidae), and a house fly Musca domestica (Muscidae), on the other hand, had divided 5.8S rRNA as did a fruit fly Drosophila melanogaster (Drosophilidae) and a dark-winged fungus gnat Sciara coprophila (Sciaridae). Three hypotheses are proposed on the relationship between the evolution of the 5.8S rRNA and the phylogeny of Diptera.
Animals↗
Gene structure of Bombyx mori larval serum protein (BmLSP).
To understand the molecular mechanisms of the larval-specific transcription of Bombyx mori larval serum protein (BmLSP), we isolated a clone of the BmLSP gene from a genomic library and sequenced a 3.5-kb fragment. An intron was found in the 5' noncoding region of the BmLSP gene. A putative transcription start point was determined by primer extension analysis. Genomic Southern hybridization showed that there is one copy of the BmLSP gene in a haploid genome. A database search revealed that the BmLSP gene has presumptive repetitive sequences found in other B. mori genes, the sequence homologous to ecdysone-responsive elements and a heptamer sequence found in storage protein genes.
Amino Acid Sequence↗
Function-informed transcriptome analysis of Drosophila renal tubule.
BACKGROUND: Comprehensive, tissue-specific, microarray analysis is a potent tool for the identification of tightly defined expression patterns that might be missed in whole-organism scans. We applied such an analysis to Drosophila melanogaster Malpighian (renal) tubule, a defined differentiated tissue. RESULTS: The transcriptome of the D. melanogaster Malpighian tubule is highly reproducible and significantly different from that obtained from whole-organism arrays. More than 200 genes are more than 10-fold enriched and over 1,000 are significantly enriched. Of the top 200 genes, only 18 have previously been named, and only 45% have even estimates of function. In addition, 30 transcription factors, not previously implicated in tubule development, are shown to be enriched in adult tubule, and their expression patterns respect precisely the domains and cell types previously identified by enhancer trapping. Of Drosophila genes with close human disease homologs, 50 are enriched threefold or more, and eight enriched 10-fold or more, in tubule. Intriguingly, several of these diseases have human renal phenotypes, implying close conservation of renal function across 400 million years of divergent evolution. CONCLUSIONS: From those genes that are identifiable, a radically new view of the function of the tubule, emphasizing solute transport rather than fluid secretion, can be obtained. The results illustrate the phenotype gap: historically, the effort expended on a model organism has tended to concentrate on a relatively small set of processes, rather than on the spread of genes in the genome.
Animals↗
The consequences of ubiquitous expression of the wingless gene in the Drosophila embryo.
The segment polarity gene wingless has an essential function in cell-to-cell communication during various stages of Drosophila development. The wingless gene encodes a secreted protein that affects gene expression in surrounding cells but does not spread far from the cells where it is made. In larvae, wingless is necessary to generate naked cuticle in a restricted part of each segment. To test whether the local accumulation of wingless is essential for its function, we made transgenic flies that express wingless under the control of a hsp70 promoter (HS-wg flies). Uniform wingless expression results in a complete naked cuticle, uniform armadillo accumulation and broadening of the engrailed domain. The expression patterns of patched, cubitus interruptus Dominant and Ultrabithorax follow the change in engrailed. The phenotype of heatshocked HS-wg embryos resembles the segment polarity mutant naked, suggesting that embryos that overexpress wingless or lack the naked gene enter similar developmental pathways. The ubiquitous effects of ectopic wingless expression may indicate that most cells in the embryo can receive and interpret the wingless signal. For the development of the wild-type pattern, it is required that wingless is expressed in a subset of these cells.
Animals↗
Autocatalysis and phenotypic expression of Drosophila homeotic gene Deformed: its dependence on polarity and homeotic gene function.
Previously published experiments have shown that the endogenous Dfd gene can be ectopically activated by its own (heat-shock-driven) product in a subset of cells of different segments. This results in the differentiation of maxillary structures like cirri and mouth hooks in places where they normally do not appear, and represents a phenomenon of autocatalysis of homeotic gene function that differs from the normal activation process. We show that this out-of-context activation occurs in cells belonging to the anterior compartments of the three thoracic and the A1 to A8 abdominal segments and that it requires the normal function of the polarity genes wingless (wg) and engrailed (en). The wg product, in addition to that of Dfd, appears to be sufficient to activate the endogenous Dfd gene in many embryonic cells. We have studied the effect of several homeotic genes on Dfd activation and phenotypic expression: Scr, Antp, Ubx and Abd-B repress Dfd both transcriptionally and at the phenotypic level, if their products are in sufficient amounts. The endogenous abd-A gene does not have a noticeable effect, but when it is replaced by an hsp70-abd-A gene, which produces a high and uniform level of expression, the phenotypic expression of Dfd is suppressed. Our results also suggest that the differentiation of cirri is induced by Dfd-expressing cells in non-expressing neighboring cells, and that this interaction occurs across the parasegmental border.
Animals↗
Tissue-specific ecdysone responses: regulation of the Drosophila genes Eip28/29 and Eip40 during larval development.
The Drosophila genes Eip28/29 and Eip40 are expressed in Kc cells and are rapidly induced by the steroid hormone ecdysone. The molecular basis for Eip28/29's regulation in those cells has been studied in some detail. To determine how this regulation relates to normal development, we have examined the expression of both genes throughout Drosophila development, with special attention to Eip28/29 and the final larval instar. Eip28/29 expression is complex; there are tissues in which it is never expressed, others in which it is continuously expressed at a low level and tissues in which its expression is regulated without obvious relationship to endocrine events. However high-level Eip28/29 expression always correlates with the presence of ecdysone and there is good evidence that Eip28/29 is directly regulated by the hormone in some tissues and at some stages. Most striking are the induction of Eip28/29 transcripts in numerous tissues at the last larval molt, their induction in the epidermis at the time of the 'late 3rd transition', their extinction in the same tissue by the premetamorphic ecdysone peak, and their induction by that peak in the lymph gland, hemocytes and proventriculus. These contrasting regulatory behaviors provide a well-defined model for studying the developmental specificity of steroid responses. Eip40 appears to be ecdysone-inducible only in the lymph gland and there only at the premetamorphic peak. The similarities been Eip28/29 and Eip40 regulation in the lymph gland and Kc cells support the idea that Kc cells are derived from a hematopoietic ancestor.
Animals↗
The fat facets gene is required for Drosophila eye and embryo development.
In a screen for mutations affecting Drosophila eye development, we have identified a gene called fat facets (faf) which is required for cell interactions that prevent particular cells in the developing eye from becoming photoreceptors. Analysis of eyes mosaic for faf+ and faf- cells shows that faf is required in cells near to, but outside, normal developing photoreceptors and also outside of the ectopic photoreceptors in mutant facets. faf is also essential during oogenesis, and we show that a faf-lacZ hybrid protein is localized via the first 392 amino acids of faf to the posterior pole of oocytes. Posterior localization of faf-lacZ depends on oskar. oskar encodes a key organizer of the pole plasm, a specialized cytoplasm at the posterior pole of embryos. The pole plasm is required for germ cell formation and contains the determinant of posterior polarity, encoded by nanos. Although other pole plasm components are required for localization of nanos RNA or for nanos protein function, faf is not. We have cloned the faf gene, and have shown that it encodes two similar large (approximately 300 x 10(3) M(r)) proteins that are unique with respect to other known proteins.
Amino Acid Sequence↗
Isolation and functional comparison of Dmyd, the Drosophila homologue of the vertebrate myogenic determination genes, with CMD1.
We have isolated a cDNA clone, called Dmyd for Drosophila myogenic determination gene, from a 0-16 hour Drosophila embryo library that encodes a protein with structural and functional characteristics similar to the members of the vertebrate MyoD family (Paterson et al 1991). Dmyd encodes a polypeptide of 332 amino acids with 82% identity to MyoD in the 41 amino acids of the putative helix-loop-helix region and 100% identity in the 13 amino acids of the basic domain proposed to contain the essential recognition code for muscle specific gene activation. The gene is unique and maps to 95A/B on the right arm of the third chromosome. Low stringency hybridizations indicate Dmyd is not a member of a multigene family, similar to MyoD in vertebrates. Dmyd is a nuclear protein in Drosophila, consistent with its role as a nuclear gene regulatory factor, and is proposed to be a transiently expressed marker for a unique subset of muscle founder cells. We have used an 8kb promoter fragment from the gene, which contains the first 55 amino acids of the Dmyd protein, joined to lac Z to follow myogenic precursor cells into muscle fibers using antibodies to beta-galactosidase and Dmyd. Unlike the myogenic factors in vertebrate muscle cells, Dmyd appears to be expressed at a much lower level in differentiated Drosophila muscles so it cannot be followed continuously as a muscle marker. This is reflected in the loss of expression of Dmyd RNA in 12-24 hour embryos, a major period of early myogenesis, as well as in the undetectable level of the nuclear antigen in primary cultures of embryonic and adult Drosophila muscle. Functional differences between Dmyd and CMD1 are described and explained in terms of a model which may give insight to the nature of homo and heterodimer formation in the bHLH family of proteins.
Amino Acid Sequence↗
Molecular cloning and characterization of the genes encoding the two subunits of Drosophila melanogaster calcineurin.
Genomic clones containing the full coding sequences of the two subunits of the Ca2+/calmodulin-stimulated protein phosphatase, calcineurin, were isolated from a Drosophila melanogaster genomic library using highly conserved human cDNA probes. Three clones encoded a 19.3-kDa protein whose sequence is 88% identical to that of human calcineurin B, the Ca(2+)-binding regulatory subunit of calcineurin. The coding sequences of the Drosophila and human calcineurin B genes are 69% identical. Drosophila calcineurin B is the product of a single intron-less gene located at position 4F on the X chromosome. Drosophila genomic clones encoding a highly conserved region of calcineurin A, the catalytic subunit of calcineurin, were used to locate the calcineurin A gene at position 21 EF on the second chromosome of Drosophila and to isolate calcineurin A cDNA clones from a Drosophila embryonic cDNA library. The structure of the calcineurin A gene was determined by comparison of the genomic and cDNA sequences. Twelve exons, spread over a total of 6.6 kilobases, were found to encode a 64.6-kDa protein 73% identical to either human calcineurin A alpha or beta. At the nucleotide level Drosophila calcineurin A cDNA is 67 and 65% identical to human calcineurin A alpha and beta cDNAs, respectively. Major differences between human and Drosophila calcineurins A are restricted to the amino and carboxyl termini, including two stretches of repetitive sequences in the carboxyl-terminal third of the Drosophila molecule. Motifs characteristic of the putative catalytic centers of protein phosphatase-1 and -2A and calcineurin are almost perfectly conserved. The calmodulin-binding and auto-inhibitory domains, characteristic of all mammalian calcineurins A, are also conserved. A remarkable feature of the calcineurin A gene is the location of the intron/exon junctions at the boundaries of the functional domains and the apparent conservation of the intron/exon junctions from Drosophila to man.
Amino Acid Sequence↗