0000000001264475

AUTHOR

Viviane Jaenicke

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Characterization of DrosophilaHemoglobin

2002

In contrast to previous assumptions, the fruit fly Drosophila melanogaster possesses hemoglobin. This respiratory protein forms a monomer of about 17 kDa that is not exported into the hemolymph. Recombinant Drosophila hemoglobin displays a typical hexacoordinated deoxy spectrum and binds oxygen with an affinity of 0.12 torr. Four different hemoglobin transcripts have been identified, which are generated by two distinct promoters of the hemoglobin (glob1) gene but are identical in their coding regions. Putative binding sites for hypoxia-regulated transcription factors have been identified in the gene. Hemoglobin synthesis in Drosophila is mainly associated with the tracheal system and the fa…

biologyfungiOxygen transportPromoterCell Biologybiology.organism_classificationBiochemistryRespiratory proteinBiochemistryHemolymphHemoglobinBinding siteDrosophila melanogasterMolecular BiologyTranscription factorJournal of Biological Chemistry
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