0000000000361384

AUTHOR

Sabine Klawitter

showing 3 related works from this author

The hemoglobin genes of Drosophila

2006

We recently reported the unprecedented occurrence of a hemoglobin gene (glob1) in the fruitfly Drosophila melanogaster. Here we investigate the structure and evolution of the glob1 gene in other Drosophila species. We cloned and sequenced glob1 genes and cDNA from D. pseudoobscura and D. virilis, and identified the glob1 gene sequences of D. simulans, D. yakuba, D. erecta, D. ananassae, D. mojavensis and D. grimshawi in the databases. Gene structure (introns in helix positions D7.0 and G7.0), gene synteny and sequence of glob1 are highly conserved, with high ds/dn ratios indicating strong purifying selection. The data suggest an important role of the glob1 protein in Drosophila, which may b…

Molecular Sequence DataSequence alignmentBiologyBiochemistryConserved sequenceEvolution MolecularHemoglobinsDrosophilidaeAnimalsDrosophila ProteinsGuanine Nucleotide Exchange FactorsAmino Acid SequenceGlobinCloning MolecularMolecular BiologyGeneConserved SequencePhylogenySyntenyGeneticsSequence Homology Amino AcidfungiIntronCell Biologybiology.organism_classificationDrosophilaDrosophila melanogasterSequence AlignmentFEBS Journal
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Characterization of two globin genes from the malaria mosquito Anopheles gambiae: Divergent origin of nematoceran haemoglobins

2007

The chironomid midges are the only insects that harbour true haemoglobin in their haemolymph. Here we report the identification of haemoglobin genes in two other nematoceran species. Two paralogous haemoglobin genes (glob1 and glob2) from the malaria mosquito Anopheles gambiae were cloned and sequenced. Furthermore, we identified two orthologous haemoglobin genes in the yellow fever mosquito Aedes aegypti. All four haemoglobins were predicted to be intracellular proteins, with the amino acids required for heme- and oxygen-binding being conserved. In situ-hybridization studies showed that glob1 and glob2 expression in An. gambiae is mainly associated with the tracheal system. This pattern re…

GeneticsAedesbiologyPhylogenetic treeAnopheles gambiaeMolecular Sequence DatafungiIntronSequence Analysis DNAAedes aegyptibiology.organism_classificationBiological EvolutionChironomidaeHemoglobinsAedesInsect ScienceAnophelesMidgeGeneticsAnimalsAmino Acid SequenceGlobinMolecular BiologyGeneInsect Molecular Biology
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Molecular characterization of hemoglobin from the honeybee Apis mellifera

2005

Due to the prevailing importance of the tracheal system for insect respiration, hemoglobins had been considered rare exceptions in this arthropod subphylum. Here we report the identification, cloning and expression analysis of a true hemoglobin gene in the honeybee Apis mellifera (Hymenoptera). The deduced amino acid sequence covers 171 residues (19.5 kDa) and harbors all globin-typical features, including the proximal and the distal histidines. The protein has no signal peptide for transmembrane transport and was predicted to localize in the cytoplasm. The honeybee hemoglobin gene shows an ancient structure, with introns in positions B12.2 and G7.0, while most other insect globins have div…

Signal peptideInsectaPhysiologymedia_common.quotation_subjectMolecular Sequence DataInsectBiologyHemoglobinsPhylogeneticsBotanyAnimalsAmino Acid SequenceRNA MessengerGlobinGenePeptide sequencemedia_commonGeneticsBase SequencefungiIntronSequence Analysis DNABeesBiological EvolutionInsect ScienceHemoglobinJournal of Insect Physiology
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