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At least 847 records · Page 47Linked to original sources
PubMed1988

Isolation of cDNA clones coding for mitochondrial 16S ribosomal RNA from the crustacean Artemia.

cDNA clones coding for Artemia mitochondrial 16S ribosomal RNA (rRNA) have been isolated. The clones cover from nucleotide 650 of the RNA molecule to its 3' end. The comparison of Artemia sequence with both vertebrate and invertebrate mitochondrial 16S rRNA sequences has shown the existence of regions of high similarity between them. A model for the secondary structure of the 3' half of Artemia mitochondrial 16S rRNA is proposed. The size of the rRNA molecule has been estimated at 1.35 kb. Despite the similarity of the Artemia gene to insect rRNA in size, sequence and secondary structure, the G + C content of the Artemia gene (42%) is closer to that of mammals than to the insect genes. The number of mitochondria in Artemia has been estimated at 1500 per diploid genome in the cyst and 4000 in the nauplius. In contrast, the amount of mt 16S rRNA is constant at all stages of Artemia development.

Animals↗
PubMed2002

The odorant-binding proteins of Drosophila melanogaster: annotation and characterization of a divergent gene family.

Insect odorant-binding proteins (OBPs) are thought to facilitate the delivery of hydrophobic odorants, such as sex pheromones or food odors, to receptors on sensory neurons. Increasingly, OBP family members are also being found in non-sensory tissues where they might carry other types of small hydrophobic molecules. They are identifiable by four or six conserved Cys residues and contain six alpha-helices which enclose a hydrophobic ligand-binding pocket. Through exhaustive BLAST searches we have increased the total number of OBPs identified in Drosophila melanogaster to 38, and have amplified the DNA complementary to RNA corresponding to 21 of these by reverse transcriptase polymerase chain reaction. Isoforms frequently share less than 30% amino acid identity and appear to have radically changed since the separation of the major insect orders. However, their sequences are consistent with known OBP structures. Most are located in clusters of between four and 14 genes and several were unusual in that they contained additions, deletions, or fusions. These hexa-helical insect OBPs are structurally unrelated to the functionally analogous lipocalin-like beta-barrel OBPs of vertebrates. As only two lipocalin-like proteins have been found in D. melanogaster, these helical proteins appear to be the dominant carrier of small hydrophobic molecules in insects.

Amino Acid Sequence↗
PubMed2005

Envelope gene capture and insect retrovirus evolution: the relationship between errantivirus and baculovirus envelope proteins.

In this report the evolution of insect retroviruses (errantiviruses) is reviewed with particular emphasis on the relationship between their env protein and a baculovirus envelope fusion protein. In addition, selected features of the env protein from the errantivirus Dme17.6V are examined. These include characterization of the 21 amino acid predicted fusion peptide sequence that is highly homologous to a region of baculovirus envelope fusion proteins. We found that, although this sequence could not substitute for the homologous sequence in the baculovirus LD130 envelope fusion protein, by changing four amino acids, the hybrid construct became active for low-pH induced cell fusion. In addition, a Dme17.6V env-egfp construct was found to localize to cell membranes.

Amino Acid Sequence↗
PubMed1999

[Western blotting of RStV gene products in rice and insects].

The NS3 and NC protein genes encoded by RNA3 of RStV, the NCP and NSvc4 protein genes encoded by RNA4 were subcloned into the E. coli expression vector pGEX3X to express four groups of fusion protein under IPTG induction. These fusion proteins were used to immunize rabbits to raise antisera. The antisera against the E. coli-expressed proteins were available for probing the presence of the viral gene products in both rice plant and insect hosts. The expected gene products can be probed only in diseased rice plant with NCP antiserum and the corresponding products detected in both plant and RStV particle preparation with NC antiserum. The viral gene products probed by NS3 and NSvc4 antisera were different from the expected ones in size.

Animals↗
PubMed2005

Galatosylation and sialylation of mammalian glycoproteins produced by baculovirus-madiated gene expression in insect cells.

The baculovirus expression vector system (BEVS) is used extensively for the production of proteins from exogenous cDNAs. However, BEVS is not ideal for pharmaceutical production of glycoproteins owing to the properties of the N-glycans in the expressed products and that insect cells lack several of the enzymes required for mammalian-type N-glycan synthesis. This study describes the effective mammalian-like production of glycoproteins, such as beta-1,4-galactosyltransferase and alpha-2,6-sialyltransferase, in the insect cell line Sf9.

Animals↗
PubMed1993

Immune reactions in Drosophila and other insects: a model for innate immunity.

All insects defend themselves against bacteria and parasites, using cellular and humoral systems that are rapidly activated in infected animals. Among the induced effector molecules are antibacterial proteins and peptides such as cecropins, attacins, lysozymes and insect defensins, the genes for many of which have now been cloned. The induction of this system, which lacks clonally selected receptors like those of vertebrate B and T cells, may provide a model for innate immune reactions in other animals, including vertebrates.

Amino Acid Sequence↗
PubMed1991

An amplified insect dihydrofolate reductase gene contains a single intron.

We have used methotrexate-resistant mosquito (Aedes albopictus) cells as the source of DNA for cloning an 8.5-kb EcoRI fragment containing an amplified dihydrofolate reductase (DHRF) gene. An estimated 1200 copies of the DHFR gene were represented in nuclear DNA from Mtx-5011-256 cells, which were 3000-fold more resistant to methotrexate than wild-type cells. Southern blot analysis indicated that all of the amplified DHFR genes were contained within a 1.8-kb AccI fragment represented in the cloned DNA. In contrast to mammalian DHFR genes which span approximately 30 kb, the complete amino acid coding sequence of the mosquito DHFR gene spanned 614 nucleotides, including a single 56-nucleotide intron that interrupted a conserved Arg codon at amino acid position 27. Additional introns characteristic of mammalian DHFR genes were absent; conservation of the first intron in the mosquito DHFR gene supports a regulatory role for this intron. The mosquito DHFR gene coded for a 186-amino-acid protein with 43-48% similarity to vertebrate DHFR.

Aedes↗
PubMed1999

An Integrated View of Insect Flight Muscle: Genes, Motor Molecules, and Motion.

Substituting an alanine for serine in the regulatory subunit of the motor protein myosin dramatically alters Drosophila's flight ability. Power output, at all levels of the flight system, is reduced. This example of deciphering a protein's function by producing malfunctions illustrates the broadening use of molecular genetics in integrative biology.

Journal Article↗
PubMed1995

Structure and expression of Hemolin, an insect member of the immunoglobulin gene superfamily.

Hemolin is an insect protein which belongs to the immunoglobulin superfamily and is strongly induced upon bacterial infection. It has been isolated from two moths, Hyalophora cecropia and Manduca sexta. We have isolated and sequenced a genomic clone for hemolin in H. cecropia, in order to resolve its organization and as a basis for investigating hemolin gene regulation. According to Southern-blot analysis, hemolin is encoded by a single gene, Hemolin. It contains six exons ranging over 32-603 bp. The introns are positioned both within and between the immunoglobulin-like domains, a feature typical for cell-adhesion molecules belonging to the immunoglobulin superfamily. By an RNase protection assay, we show that the Hemolin transcript is strongly induced not only by bacteria, but also by lipopolysaccharide and phorbol 12-myristate 13-acetate. Analysis of the upstream region and introns revealed potential binding sites for the Cecropia immunoresponsive factor (CIF), which recognizes the kappa B-like consensus GGGRA YYYYY.

Amino Acid Sequence↗
PubMed1991

Prevention of apoptosis by a baculovirus gene during infection of insect cells.

Programmed cell death is an active process of self destruction that is important in both the development and maintenance of multicellular animals. The molecular mechanisms controlling activation or suppression of programmed cell death are largely unknown. Apoptosis, a morphologically and biochemically defined type of programmed cell death commonly seen in vertebrates, was found to be initiated during baculovirus replication in insect cells. A specific viral gene product, p35, was identified as being responsible for blocking the apoptotic response. Identification of the function of this gene will allow further definition of the molecular pathways involved in the regulation of programmed cell death and may identify the role of apoptosis in invertebrate viral defense systems.

Amino Acid Sequence↗
PubMed1996

Conserved promoter elements in the CYP6B gene family suggest common ancestry for cytochrome P450 monooxygenases mediating furanocoumarin detoxification.

Despite the fact that Papilio glaucus and Papilio polyxenes share no single hostplant species, both species feed to varying extents on hostplants that contain furanocoumarins. P. glaucus contains two nearly identical genes, CYP6B4v2 and CYP6B5v1, and P. polyxenes contains two related genes, CYP6B1v3 and CYP6B3v2. Except for CYP6B3v2, the substrate specificity of which has not yet been defined, each of the encoded cytochrome P450 monooxygenases (P450s) metabolizes an array of linear furanocoumarins. All four genes are transcriptionally induced in larvae by exposure to the furanocoumarin xanthotoxin; several are also induced by other furanocoumarins. Comparisons of the organizational structures of these genes indicate that all have the same intron/exon arrangement. Sequences in the promoter regions of the P. glaucus CYP6B4v2/CYP6B5v1 genes and the P. polyxenes CYP6B3v2 gene are similar but not identical to the -146 to -97 region of CYP6B1v3 gene, which contains a xanthotoxin-responsive element (XRE-xan) important for basal and xanthotoxin-inducible transcription of CYP6B1v3. Complements of the xenobiotic-responsive element (XRE-AhR) in the dioxin-inducible human and rat CYP1A1 genes also exist in all four promoters, suggesting that these genes may be regulated by dioxin. Antioxidant-responsive elements (AREs) in mouse and rat glutathione S-transferase genes and the Barbie box element (Bar) in the bacterial CYP102 gene exist in the CYP6B1v3, CYP6B4v2, and CYP6B5v1 promoters. Similarities in the protein sequences, intron positions, and xanthotoxin- and xenobiotic-responsive promoter elements indicate that these insect CYP6B genes are derived from a common ancestral gene. Evolutionary comparisons between these P450 genes are the first available for a group of insect genes transcriptionally regulated by hostplant allelochemicals and provide insights into the process by which insects evolve specialized feeding habits.

Amino Acid Sequence↗